Advancements in bio/nano-technology require insights from studies of biology at the molecular level. We, Separovic Lab @ Bio21, study the biophysical chemistry of membrane-active peptides and proteins relevant to disease states and treatments.

The structure-function relationships of macromolecular assemblies at the atomistic level are examined using solid-state nuclear magnetic resonance (NMR) methods to determine the structure and dynamics of protein complexes and biological membranes.

NMR spectroscopy, complemented by a range of biophysical techniques, is being used to determine the mechanism of action of membrane polypeptides. Our primary goal is to do this for membrane components in situ. We have determined the 3D structure of peptides, the antibiotic gramicidin A and the bee toxin melittin, in phospholipid membranes using solid-state NMR methods that are now being extended to membrane proteins.

Together with other multidisciplinary research groups we investigate biological macromolecules, geopolymers and ionic liquids for pharmaceutical & industrial applications. Current focus is on the structure & interactions of amyloid peptides from Alzheimer’s disease, pore-forming toxins and antibiotic peptides in biological membranes.

LinkedIn
Twitter

NMR & Membrane Biophysics Group comprises:

• Dr Frances Separovic AO, FAA (Distinguished Professor Emeritus)
• Dr Marc-Antoine Sani – Senior Research Fellow, Bio21 Institute
• Prof. Graham Jackson – Visiting Researcher, UCT
• Dr Fazel Shabanpoor – Visiting Researcher, HFI
• Haoning Gong – Visiting PhD student, UOM
• Nikolina Kalcec – Visiting PhD student, UNIZG

Our laboratory is located at the Bio21 Institute. See our group page.

Some of our former group members, and their positions:

• Dr Shiying Zhu: post-doc, Biochemistry & Molecular Biology, Monash University
• Dr Behnoosh Tajik: scientist, CSL Limited, Melbourne
• Dr Thomas Meikle: post-doc, School of Science, RMIT University, Melbourne
• Dr Sarah Overall: post-doc, Chemistry & Biochemistry, University of California Santa Cruz
• Dr Nitin Patil: post-doc, Florey Institute for Neuroscience & Mental Health, Melbourne
• Dr Wenyi Li: post-doc, Leibnitz Institute for Molecular Pharmacology, FMP-Berlin
• Dr Anna Mularski: OPCW, The Hague; post-doc, Institut Cochin, Paris
• Dr John Karas: post-doc, Chemical & Biomolecular Engineering, University of Melbourne
• Dr Daniel Weber: post-doc, IBM Research – Australia; Biochem, Mol Biol & Biophys, University of Minnesota
• Dr Vino Nair: Bain India; KPMG Australia
• Dr John Gehman: ARC Future Fellow, Chemistry, University of Melbourne
• Dr Linda Chan: post-doc, Monash Institute of Pharmaceutical Sciences
• Dr David Fernandez: Australian Defence Force
• Mr Tom Whitwell (MSc): Masters student, Graduate School of Business & Economics
• Dr Scott Fraser: National Product Specialist in Thermal Analysis, PerkinElmer
• Dr Geoff Burrell: The Technology Centre, DuluxGroup (Australia) Pty Ltd
• Dr Fazel Shabanpoor: CJ Martin Fellow, Howard Florey Institute & University of Cambridge
• Ms Caitlin O’Brien (Hons): Orica Graduate Program; Dulux
• Dr Martin Boland: senior lecturer, Charles Darwin University
• Dr Alison Drechsler: science teacher, QLD
• Dr Crystal Tong Lay Lau: post-doc, Keck School of Medicine, University of Southern California; Health Science Authority, Singapore
• Dr Maurits de Planque: lecturer, Electronics & Computing Sciences, University of Southampton
• Dr Anna Tickler: post-doc, Cavendish Laboratory, Cambridge University; Mimotopes
• Dr Feda’ Ali: post-doc, Pathology Department, University of Melbourne; CSL
• Ms Anita Kishore (MSc): PhD student, Chemistry Department, University of Georgia; consultant, Bain & Co.
• Dr Aphrodite Anastasiadis-Poole: post-doc, Goethe Universitaet Frankfurt; scientific recruitment consultant, Kelly Scientific Resources
• Dr Yuen-Han (Tracy) Lam: post-doc, Biochemistry Department, University of Oxford
• Dr Craig Morton: principal research scientist, Biota Structural Biology, Melbourne

Frances Separovic is Distinguished Professor Emeritus of Chemistry, Deputy Director of the Bio21 Institute and former Head of School at the University of Melbourne. Frances was a Visiting Professor at Harvard Medical School, Honorary Fellow of Birkbeck College UCL, and a Senior Member of St Hugh’s College, Oxford. Frances has a BA (Hons) in Math & Physics from Macquarie University and a PhD (Physics) from University of NSW. Her tertiary training in biology, mathematics and physics, provides a strong foundation for research in biophysical chemistry and NMR spectroscopy.

Her primary research interest is determination of the structure & dynamics of membrane components in situ using solid-state NMR spectroscopy. Frances played a key role in determining the molecular structure of the antibiotic gramicidin A and the bee toxin melittin within phospholipid membranes. Using novel solid-state NMR methods Frances was able to determine the structure & dynamics of membrane polypeptides for biomolecular engineering applications.

She is very active in the area of membrane biophysics and structural biology and is Past President of the Biophysical Society, Foreign Secretary of the Australian Academy of Science, former President of Australian & New Zealand Society for Magnetic Resonance (ANZMAG) and the Australian Society for Biophysics (ASB); a committee member of International Society for Magnetic Resonance (ISMAR); and former treasurer of the Royal Australian Chemical Institute (RACI) and the Lorne Protein Conference.

Frances has organized over 50 major national & international conferences and published over 250 peer reviewed papers. Her contributions to biophysics and NMR have been recognized by award of the 2009 ASB Robertson Medal and 2011 ANZMAG Medal. In 2012 she was elected a Fellow of the Biophysical Society, Fellow of the Australian Academy of Science (FAA) and an ISMAR Fellow; in 2017 Frances was named an IUPAC Distinguished Woman of Chemistry/Chemical Engineering and in 2018 inducted in the Victorian Honour Roll of Women; and appointed an Officer of the Order of Australia (AO) in 2019.

School of Chemistry Academic Staff list. Contact fs @ unimelb.edu.au

Separovic Career Profile and LinkedIn

Media links and Twitter

Rosalba Kampman Distinguished Service Award, BPS Bulletin 2024 Society Awards, Oct 2023

The Protein Society newsletter, Under the Microscope Member Spotlight, Nov 2022

Womanthology interview Diversity drives science forward!, Feb 2022

Biophysical Society newsletter, BPS Bulletin Biophysicist in Profile, Feb 2021

New book, ‘Solid-State NMR: Applications in Biomembrane Structure’, Dec 2020

Scientists Without Labels profile, August 2020

Metro Tunnel VIC art work Parkville Storytelling Project, Feb 2020

IUPAC Global Women’s Breakfast 2020 video interview

STEMinists in Antarctica Barrier Daily Truth OpEd, Feb 2020

Frances receives RACI Margaret Sheil Leadership Award

Hello Bio career interview with Frances

Australian Academy of Science career video on Frances

Frances, President-elect of Biophysical Society, BPS election results

Interview on STEM Women database, SBS News link and video

Deputy-director reflects on IUPAC & IYPT Bio21 Digest, Aug 2019

‘When an artist looks at a chemical element, what do they see?’, The Conversation, Jul 2019

Deputy-director on Diversity & Inclusion Bio21 2018 Annual Report

‘Officer of the Order of Australia (AO)’, Queen’s Birthday Honours 2019 and BDT article

‘Alumnae off to Antarctica with women leadership program’, UNSW Newsroom article

‘Peptide antibiotics from frog skin’, ABC Illawarra Drivetime chat, Mar 2019

‘Don’t ask women leaders to act like men’ International Women’s Day 2019, interview

The Year That Made Me: Frances Separovic 1996, ABC Radio National interview, October 2018

The Advocate NTEU interview, Jul 2018

Barrier Daily Truth Broken Hill interview, May 2018

Eavesdrop on Experts podcast: ‘Smashing through science’s glass ceiling’

Women in STEMM Australia STEMM Profile

Induction as a Trailblazer for Women in Science into Victorian Honour Roll of Women; see stories of 2018 Awardees and group photo. Read the ‘Pursuit‘ article

International Women’s Day 2018 Award

Deputy-director on Women of Bio21 Bio21 2017 Annual Report

Frances featured as University of Melbourne scientist on Croatian TV (HTV1)

Women leaders, President of Croatia visits Bio21, Aug 2017

2017 UNSW Alumni Science & Technology Award UNSW celebrates its star graduates

Distinguished Women in Chemistry IUPAC 2017 Award

ANZMAGazine interview, Dec 2016

Celebrating arrival of DNP-NMR

Address at Gender Equity forum

Frances reflects on Head of School interview

Get to know Frances Separovic, new BPS Secretary

New NMR installed: Everyday quantum mechanics & the study of cell membranes

Frances elected Secretary of Biophysical Society

Voice interview, The chemistry of curiosity, May 2014

New book, ‘Advances in Biological Solid-State NMR: Proteins & Membrane-Active Peptides’

Up Close episode 272, interview: Pore me another: Understanding how toxins target & overcome membranes, Oct 2013

Maths of Planet Earth interview See article, May 2013

Frances elected 2012 ISMAR Fellow

Bluestocking Interview in ‘The Advocate‘, Nov 2012

Frances elected to Australian Academy of Science  UniNews ARC news

Frogs thwart superbugs in the news: SMH, ABC, UniMelb, The Age

Frances Fellow of Biophysical Society See press release

Celebrating our women in science interview – 2011 ANZMAG Medal 

Chemistry in Australia interview: 2009 Robertson Medal

Profiled in Biophysical Society Newsletter, Apr 2009

Interview in ‘Croatian Herald‘, 29 Jan 2007

1. “Recent studies of lyotropic lipidic cubic phases.” Yao, S., Meikle, T.G., Separovic, F. and Keizer, D.W. (2023) Annu. Rep. on NMR Spectrosc. 110, 31-78.
2. “Selenium nanoparticles as potential drug delivery systems for the treatment of Parkinson’s disease: Case studies of L-DOPA and dopamine.” Kalčec, N., Peranić, N., Mamić, I., Beus, M., Hall, C., Smith, T., Sani, M.-A., Turčić, P., Separovic, F. and Vinković Vrček, I. (2023) ACS Appl. Nano Mater. 6, 17581-17592.
3. “The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent.” Sani, M.-A., Le Brun, A.P., Rajput, S., Attard, T. and Separovic, F. (2023) Biophys. J. 122, 1058-1067.
4. “A solution NMR view of lipidic cubic phases: Structure, dynamics, and beyond.” Meikle, T.G., Keizer, D.W., Separovic, F. and Yao, S. (2022) BBA Adv. 2, 100062 (11 pages).
5. “In-cell DNP NMR reveals multiple targeting effect of antimicrobial peptide.” Separovic, F., Hofferek, V., Duff, A., McConville, M.J. and Sani, M.-A. (2022) J. Struct. Biol.: X 6, 100074 (6 pages).
6. “Transformation of L-DOPA and dopamine on the surface of gold nanoparticles: An NMR and computational study.” Kalčec, N., Ljulj, A., Božičević, L., Vrček, V., Marson, D., Pricl, S., Separovic, F. and Vinković Vrček, I. (2022) Inorg. Chem. 61, 10781-10791.
7. “Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals.” Pathak, R., Bhangu, S.K., Martin. G.J.O., Separovic, F. and Ashokkumar, M. (2022) Eur. Biophys. J. 51, 335-352.
8. “NMR measurement of biomolecular translational and rotational motion for evaluating changes of protein oligomeric state in solution.” Yao, S., Keizer, D.W., Babon, J.J. and Separovic, F. (2022) Eur. Biophys. J. 51, 193-204.
9. “NMR spectroscopy of lipidic cubic phases.” Rajput, S., Yao, S., Keizer, D., Sani, M.-A. and Separovic, F. (2022) Biophys. Rev. 14, 67-74.
10. “Multi-omic analysis to characterize metabolic adaptation of the E. coli lipidome in response to environmental stress.” Kralj, T., Nuske, M., Hofferek, V., Sani, M.-A., Separovic, F., Lee, T.-H., Aguilar, M.-I. and Reid, G.E. (2022) Metabolites 12, 171 (16 pages).
11. “Enhancing proline-rich antimicrobial peptide action by homodimerization: Influence of bifunctional linker.” Li, W., Lin, F., Hung, A., Barlow, A., Sani, M.-A., Paolini, R., Singleton, W., Holden, J., Hossain, M.A., Separovic, F., O’Brien-Simpson N.M. and Wade, J.D. (2022) Chem. Sci. 13, 2226-2237.
12. “Peptide multimerization as leads for therapeutic development.” Sheard, D.E., Li, W., O’Brien-Simpson, N.M., Separovic, F. and Wade, J.D. (2022) Biologics 2, 15-44.
13. “Spectroscopic study of L-DOPA and dopamine binding on novel gold nanoparticles towards more efficient drug-delivery system for Parkinson’s disease.” Kalčec, N., Peranić, N., Barbir, R., Hall, C.R., Smith, T.A., Sani, M.-A., Frkanec, R., Separovic, F. and Vinković Vrček, I. (2022) Spectrochim. Acta A 268, 120707 (13 pages).
14. “Characterisation of cell membrane interaction mechanisms of antimicrobial peptides by electrical bilayer recording.” Priyadarshini, D., Ivica, J., Separovic, F. and de Planque, M. (2022) Biophys. Chem., 281, 106721 (7 pages).
15. “Water diffusion in complex systems measured by PGSE-NMR using chemical shift selective stimulated echo: Elimination of magnetization exchange effects.” Meikle, T., Keizer, D.W., Separovic, F. and Yao, S. (2021) J. Chem. Phys. 155, 22403 (8 pages).
16. “The impact of antibacterial peptides on bacterial lipid membranes depends on stage of growth.” Lee, T.H., Hofferek, V., Sani, M.-A., Separovic, F., Reid, G.E. and Aguilar, M.-I. (2022) Faraday Discuss. 232, 399-418.
17. “TOAC spin-labelled peptides tailored for DNP-NMR studies in lipid membrane environments.” Zhu, S., Kachooei, E., Harmer, J.R., Brown, L.J., Separovic, F. and Sani, M.-A. (2021) Biophys. J. 120, 4501-4511.
18. “Expression and purification of the native C-amidated antimicrobial peptide maculatin 1.1.” Zhu, S., Weber, D.K., Separovic, F. and Sani, M.-A. (2021) J. Pept. Sci. 27, e3330 (8 pages).
19. “Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides.” Rajput, S., Sani, M.-A., Keizer, D.W. and Separovic, F. (2021) Biochem. Soc. Trans. 49, 1457-1465.
20. “Structural disruptions of the outer membranes of Gram-negative bacteria by rationally designed amphiphilic antimicrobial peptides.” Gong, H., Hu, X., Liao, M., Fa, K., Ciumac, D., Clifton, L., Sani, M.-A., King, S.M., Maestro, A., Separovic, F., Waigh, T.A., Xu, H., McBain, A.J. and Lu, J.R. (2021) ACS Appl. Mater. Interfaces 13, 16062-16074.
21. “C-terminus amidation influences biological activity and membrane interaction of maculatin 1.1.” Zhu, S., Li, W., O’Brien-Simpson, N.M., Separovic, F. and Sani, M.-A. (2021) Amino Acids 53, 769-777.
22. “Polarization transfer to external nuclear spins using ensembles of nitrogen-vacancy centers.” Healey, A.J., Hall, L.T., White, G.A.L., Teraji, T., Sani, M.-A., Separovic, F., Tetienne, J.-P. and Hollenberg, L.C.L. (2021) Phys. Rev. Appl. 15, 054052 (16 pages). arXiv:2101.12325
23. “In-cell solid-state NMR analysis of membrane proteins.” Zhu, S., Sani, M.-A. and Separovic, F. (2021) Aust. J. Chem. 74, 362-363.
24. “Chemically modified and conjugated antimicrobial peptides against superbugs.” Li, W., Separovic, F., O’Brien-Simpson, N.M. and Wade, J.D. (2021) Chem. Soc. Rev. 50, 4932-4973.
25. “Chemical exchange of hydroxyl groups in lipidic cubic phases characterised by NMR.” Meikle, T.G., Keizer, D.W., Babon, J.J., Drummond, C.J., Separovic, F., Conn, C.E. and Yao, S. (2021) J. Phys. Chem. B 125, 571-580.
26. “Prospects for nuclear spin hyperpolarisation of molecular samples using nitrogen-vacancy centres in diamond.” Tetienne, J.-P., Hall, L.T., Healey, A.J., White, G.A.L., Sani, M.-A., Separovic, F. and Hollenberg, L.C.L. (2021) Phys. Rev. B 103, 014434 (17 pages). arXiv:2008.12417
27. “NMR chemical shift and methylation of 4-nitroimidazole: Experiment and theory.” Backler, F., Sani, M.-A., Separovic, F., Vasilyev, V. and Wang, F. (2021) Aust. J. Chem. 74, 48-55.
28. “How do self-assembling antimicrobial CxGy lipopeptides kill bacteria?” Gong, H., Sani, M.-A., Hu, Z., Ke, F., Hart, J.W., Liao, M., Hollowell, P., Carter, J., Clifton, L.A., Campana, M., Li, P., King, S.M., Webster, J.R.P., Maestro, A., Zhu, S., Separovic, F., Waigh, T.A., Xu, H., McBain, A.J. and Lu, J.R. (2020) ACS Appl. Mater. Interfaces 12, 55675-55687.
29. “In-cell solid-state NMR studies of antimicrobial peptides.” Separovic, F., Keizer, D.W. and Sani, M.-A. (2020) Front. Med. Technol. 2, 610203 (7 pages).
30. “(Re)defining the proline-rich antimicrobial peptide family and the identification of putative new members.” Welch, N.G., Li, W., Hossain, M.A., Separovic, F., O’Brien-Simpson, N.M. and Wade, J.D. (2020) Front. Chem. 8, 1157 (12 pages).
31. “Solid-state NMR: Applications in Biomembrane Structure.” eds. Sani, M.-A.and Separovic, F. (2020), IOP Publishing, Bristol, U.K. pp 416.
32. “Preface.” Sani, M.-A.and Separovic, F. (2020) in Solid-state NMR: Applications in Biomembrane Structure, eds. M.-A. Sani and Separovic, F. IOP Publishing, Bristol, U.K. p xiv.
33. “Women in Chemistry 2020.” (foreword) Separovic, F. (2020) Aust. J. Chem. 73, 823-824.
34. “Physiochemical characterization and stability of lipidic cubic phases by solution NMR.” Meikle, T.G., Keizer, D.W., Babon, J.J., Drummond, C.J., Separovic, F., Conn C.E. and Yao, S. (2020) Langmuir 36, 6254-6260.
35. “The location of the antimicrobial peptide maculatin 1.1 in model bacterial membranes.” Le Brun, A.P., Zhu, S., Sani, M.-A. and Separovic, F. (2020) Front. Chem. 8, 572 (15 pages).
36. “A multi-functional surfactant catalyst inspired by hydrolases.” Nothling, M.D., Xiao, Z., Hill, N., Blyth, M.T., Bhaskaran, A., Sani, M.-A., Espinosa-Gomez, A., Ngov, K., White, J., Buscher, T., Separovic, F., O’Mara, M., Coote, M. and Connal L.A. (2020) Sci. Adv. 14, eaaz0404 (12 pages).
37. “The antimicrobial peptide maculatin self assembles in parallel to form a pore in phospholipid bilayers.” Sani, M.-A., Le Brun, A.P. and Separovic, F. (2020) Biochim. Biophys. Acta 1862, 183204 (11 pages)
38. “The conformations of virginiamycin M1 diacetate, an inhibitor of guinea pig brain CCK-B receptors, in selected solvents.” Walsworth, K., Bender, A., Separovic, F., Bergdahl, B.M. and Metzger, R.P. (2020) Aust. J. Chem. 73, 230-235.
39. “Phote-HrTH (Phormia terraenovae hypertrehalosaemic hormone), the metabolic hormone of the fruit fly: solution structure and receptor binding model.” Abdulganiyyu, I.A., Sani, M.-A., Separovic, F., Marco, H. and Jackson, G.E. (2020) Aust. J. Chem. 73, 202-211.
40. “Heteronuclear NMR spectroscopy of proteins encapsulated in cubic phase lipids.” Meikle, T.G., Sethi, A., Keizer, D.W., Babon, J.J., Separovic, F., Gooley, P.R., Conn, C.E. and Yao, S. (2019) J. Magn. Reson. 305, 146-151.
41. “Nitroxide spin labelled peptides for DNP-NMR in-cell studies.” Sani, M.-A., Zhu, S., Hofferek, V. and Separovic, F. (2019) FASEB. J. 33, 11021-11027.
42. “Cholesterol-dependent cytolysins: membrane and protein structural requirements for pore formation.” Morton, C.J., Sani, M.-A., Parker, M.W. and Separovic, F. (2019) Chem. Rev. 119, 7721-7736.
43. “The role of bacterial lipid diversity and membrane properties in modulating antimicrobial peptide activity and drug resistance.” Lee, T.-H., Hofferek, V., Separovic, F., Reid, G.E. and Aguilar, M.-I. (2019) Curr. Opin. Chem. Biol. 52, 85-92.
44. “Biophysics & Structural Biology at Synchrotrons BSBS 2019 Biological NMR session.” Separovic, F. (2019) Biophys. Rev. 11, 531-532.
45. “Membrane biophysics session, ASB/ABA symposium, Melbourne.” Liu, P. and Separovic, F. (2019) Biophys. Rev. 11, 283-284.
46. “Metallo-cubosomes: Zinc-functionalized cubic nanoparticles for therapeutic nucleotide delivery.” Tajik-Ahmadabad, B., Chollet, L., White, J., Separovic, F. and Polyzos, A. (2019) Mol. Pharm. 16, 978-986.
47. “Combating bacterial resistance by combination of antibiotics with antimicrobial peptides” Sheard, D.E., O’Brien-Simpson, N.M., Wade, J.D. and Separovic, F. (2019) Pure Appl. Chem. 99, 199-209.
48. “In situ monitoring of bacteria under antimicrobial stress using 31P solid-state NMR.” Overall, S.A., Zhu, S., Hanssen, E., Separovic and Sani, M.-A. (2019) Int. J. Mol. Sci. 20, 181 (12 pages).
49. “Listeriolysin O binding affects cholesterol and phospholipid acyl chain dynamics in fluid cholesterol-rich bilayers.” Kozorog, M., Sani, M.-A., Separovic, F. and Anderluh, G. (2018) Chem. Eur. J. 24, 14220-14225.
50. “Measuring translational diffusion of 15N-enriched biomolecules in complex solutions with a simplified 1H-15N HMQC-filtered BEST sequence.” Yao, S., Meikle, T.G., Sethi, A., Separovic, F., Babon, J.J. and Keizer, D.W. (2018) Eur. Biophys. J. 47, 891-902.
51. “Effect of dimerized melittin on gastric cancer cells and antibacterial activity.” Jamasbi, E., Lucky, S.S., Wenyi Li, W., Hossain, A.H., Gopalakrishnakone, P. and Separovic, F. (2018) Amino Acids 50, 1101-1110.
52. “Elucidating the bactericidal mechanism of action of the linear antimicrobial tetrapeptide BRBR-NH2.” Lau, Q.Y., Li, J., Sani, M.-A., Sinha, S., Li, Y., Ng, F.M., Kang, C., Bhattacharjya, S., Separovic, F., Verma, C. and Chia, C.S.B. (2018) Biochim. Biophys. Acta 1860, 1517-1527.
53. “19F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes.” Kozorog, M., Sani, M.-A., Lenarčič Živković, M., Ilc, G., Hodnik, V., Separovic, F., Plavec, J. and Anderluh, G. (2018) Sci. Rep. 8, 6894 (11 pages).
54. “Aggregation kinetics in the presence of brain lipids of Aβ(1-40) cleaved from a soluble fusion protein.” Kael, M.A., Weber, D.K., Separovic, F. and Sani, M.-A. (2018) Biochim. Biophys. Acta 1860, 1681-1686.
55. “Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes.” Nguyen, K., Garcia, A., Sani, M.-A., Diaz, D., Dubey, V., Clayton, D., Poggetto, G.D., Cornelius, F., Payne, R.J., Separovic, F., Khandelia, H., and Clarke, R.J. (2018) Biochim. Biophys. Acta 1860, 1282-1291.
56. “Stability and activity of lysozyme in stoichiometric and non-stoichiometric protic ionic liquid (PIL)-water systems.” Wijaya, E.C., Separovic, F., Drummond, C.J. and Greaves, T.L. (2018) J. Chem. Phys. 148, 193838 (9 pages).
57. “Interaction of cationic antimicrobial peptides from Australian frogs with lipid membranes.” Zhu, S., Sani, M.-A. and Separovic, F. (2018) Peptide Sci. 110, e24061 (10 pages).
58. “Covalent conjugation of cationic antimicrobial peptides with a β-lactam antibiotic core.” Li, W., O’Brien-Simpson, N.M., Holden, J.A., Otvos, L., Reynolds, E.C., Separovic, F., Hossain, M.A. and Wade, J.D. (2018) Peptide Sci. 110, e24059 (9 pages).
59. “Fluorescence imaging of the interaction of amyloid beta 40 peptides with live cells and model membranes.” Jamasbi, E., Hossain, M.A., Tan, M., Separovic, F. and Ciccotosto, G.D. (2018) Biochim. Biophys. Acta 1860, 1609-1615.
60. “Structure, function and biosynthetic origin of octapeptin antibiotics active against extensively drug-resistant Gram-negative bacteria.” Velkov, T., Gallardo-Godoy, A., Swarbrick, J., Blaskovich, M.A.T., Elliott, A.G., Han, M., Thomson, P.E., Roberts, K.D., Huang, J.X., Becker, B., Butler, M.S., Lash, L.H., Henriques, S.T., Nation, R.L., Sivanesan, S., Sani, M.-A., Separovic, F., Mertens, H., Bulach, D., Seemann, T., Owen, J., Li, J. and Cooper, M.A. (2018) Cell Chem. Biol. 25, 380-391.
61. “Effect of phosphatidylcholine bilayer thickness and molecular order on the binding of the antimicrobial peptide maculatin 1.1.” Lee, T.-H., Sani, M.-A., Overall, S., Separovic, F. and Aguilar, M.-I. (2018) Biochim. Biophys. Acta 1860, 300-309.
62. “Antimicrobial peptide structure: From model membranes to live cells.” Sani, M.-A. and Separovic, F. (2018) Chem. Eur. J. 24, 286-291.
63. “Co-polyampholytes produced from RAFT polymerization of protic ionic liquids.” Fouillet, C.C.J., Greaves, T.L., Quinn, J.F., Davis, T.P., Adamcik, J., Sani, M.-A., Separovic, F., Drummond, C.J, and Mezzenga, R. (2017) Macromolecules 50, 8965-8978.
64. “Shining light on membrane proteins.” (preface) Janes, J.W. and Separovic, F. (2017) Eur. Biophys. J. 46, 597.
65. “Membrane-active peptides, IUPAB/EBSA symposium, Edinburgh.” Sanderson, J.M. and Separovic, F. (2017) Biophys. Rev. 9, 283-284.
66. “Amphiphilic lipopeptide delivery of charge-neutral splice switching phosphorodiamidate morpholino oligonucleotides in a cell model of spinal muscular atrophy.” Tajik-Ahmadabad, B., Polyzos, A., Separovic, F. and Shabanpoor, F. (2017) Int. J. Pharm. 532, 21-28.
67. “Lipidic cubic phase-induced membrane protein crystallization: interplay between lipid structure, mesophase properties, and crystallogenesis.” Zabara, A., Meikle, T.G., Trenker, R., Yao, S., Newman, J., Peat, T.S., Separovic, F., Conn, C.E., Call, M.J., Call, M.E., Landau, E.M. and Drummond, C.J. (2017) Cryst. Growth Des. 17, 5667-5674.
68. “Zinc-coordination and C-peptide complexation endogenously inhibit IAPP aggregation.” Ge, X., Kakinen, A., Gurzov, E.N., Yang, W., Pang, L., Pilkington, E.H., Nedumpully-Govindan, P., Chen, P., Separovic, F., Mezzenga, R., Davis, T.P., Ke, P.C. and Ding, F. (2017) Chem. Commun. 53, 9394-9397.
69. “Implications of peptide assemblies in amyloid diseases.” Ke, P.C., Sani, M.-A., Ding, F., Kakinen, A., Javed, I., Separovic, F., Davis, T.P. and Mezzenga, R. (2017) Chem. Soc. Rev. 46, 6492-6531.
70. “Investigating the interaction of octapeptin A3 with model bacterial membranes.” Han, M.-L., Shen, H.-H., Hansford, K.A., Schneider, E.K., Sivanesan, S., Roberts, K.D., Thompson, P.E., Le Brun, A.P., Zhu, Y., Sani, M.-A., Separovic, F., Blaskovich, M.A.T., Baker, M.A., Moskowitz, S.M., Cooper, M.A., Li, J. and Velkov, T. (2017) ACS Infect. Dis. 3, 606-619.
71. “The efficient synthesis and purification of amyloid-β(1-42) using an oligoethylene glycol-containing photocleavable lysine tag.” Karas, J.A., Noor, A., Schieber, C., Connell, T.U., Separovic, F. and Donnelly, P.S. (2017) Chem. Comm. 53, 6903-6905.
72. “Phosphorylation of full length amyloid-β peptide modulates its amyloid aggregation, cell binding and neurotoxic properties.” Jamasbi, E., Separovic, F., Hossain, M.A. and Ciccotosto, G.D. (2017) Mol. BioSystems 13, 1545-1551.
73. “Relaxin family peptides: Structure-activity relationship studies.” Patil, N.A., Rosengren, K.J., Separovic, F., Wade, J.D., Bathgate, R.A.D. and Hossain, M.A. (2017) Br. J. Pharmacol. 174, 950-961.
74. “One pathogen two stones: Are Australian tree frog antimicrobial peptides synergistic against human pathogens?” Sani, M.-A., Carne, S., Overall, S.A., Poulhazan, A. and Separovic, F. (2017) Eur. Biophys. J. 46, 639-646.
75. “Glycine substitution reduces antimicrobial activity and helical stretch of diPGLa-H in lipid micelles.” Sani, M.-A., Saenger, C., Juretic, D. and Separovic, F. (2017) J. Phys. Chem. B 121, 4817-4822.
76. “A nanomechanical study of the effects of colistin on the Klebsiella pneumoniae AJ218 capsule.” Mularski, A., Wilksch, J.J., Hanssen, E., Ji, L., Tomita, T., Pidot, S.J., Stinear, T., Separovic, F. and Strugnell, R.A. (2017) Eur. Biophys. J. 46, 351-361.
77. “Chemical synthesis and characterization of an equinatoxin II (1-85) analogue.” Karas, J.A., Sani, M.-A. and Separovic, F. (2017) Molecules 22, 559 (7 pages).
78. “Membrane-mimetic inverse bicontinuous cubic phase systems for encapsulation of peptides and proteins.” Meikle, T.G., Drummond, C.J. Separovic, F. and Conn, C.E. (2017) in Advances in Biomembranes and Lipid Self-Assembly 25, eds. A. Iglic, M. Rappolt and A. Garcia-Sáez, Elsevier Book Series, Oxford, U.K., Chapter 3, pp63-94.
79. A QCM-D and SAXS study of the interaction of functionalised lyotropic liquid crystalline lipid nanoparticles with siRNA.” Tajik-Ahmadabad, B., Mechler, A., Muir, B.W., McLean, K., Hinton, T.M., Separovic, F. and Polyzos, A. (2017) ChemBioChem 18, 921-930.
80. “Orientation and location of the cyclotide kalata B1 in phospholipid bilayers revealed by solid-state NMR.” Grage, S.L., Sani, M.-A., Cheneval, O., Henriques, S.T., Schalck, C., Heinzmann, R., Mylne, J.S., Mykhailiuk, P.K., Afonin, S., Komarov, I.V., Separovic, F., Craik, D.J. and Ulrich, A.S. (2017) Biophysical. J. 112, 630-642.
81. “Predicting the release profile of small molecules from within the ordered nanostructured lipidic bicontinuous cubic phase using translational diffusion coefficients determined by PFG-NMR.” Meikle, T.G., Yao, S., Zabara, A., Conn, C.E., Drummond, C.J. and Separovic, F. (2017) Nanoscale 9, 2471-2478.
82. “Fluorescent ion efflux screening assay for determining membrane-active peptides.” O’Brien-Simpson, N.M., Li, W., Pantarat, N., Hossain, M.A., Separovic, F., Wade, J.D. and Reynolds, E.C. (2017) Aust. J. Chem. 70, 220-228.
83. “Atomic force microscopy studies of the interaction of antimicrobial peptides with bacterial cells.” Mularski, A. and Separovic, F. (2017) Aust. J. Chem. 70, 130-137.
84. “The effect of selective D- or Nα-methyl arginine substitution on the activity of the proline-rich antimicrobial peptide, Chex1-Arg20.” Li, W., Sun, Z., O’Brien-Simpson, N.M., Otvos, L., Reynolds, E.C., Hossain, M.A., Separovic, F. and Wade, J.D. (2017) Front. Chem. 5, article 1, 5 pages.
85. “Incorporation of antimicrobial peptides in nanostructured lipid membrane mimetic bilayer cubosomes.” Meikle, T.G., Zabara, A., Waddington, L., Separovic, F., Drummond, C. and Conn, C.E. (2017) Colloids Surf., B 152, 143-151.
86. “C-terminal modification and multimerization increase the efficacy of a proline-rich antimicrobial peptide.” Li, W., O’Brien-Simpson, N., Yao, S., Tailhades, J., Reynolds, E., Dawson, R.M., Otvos, L., Hossain, M.A., Separovic, F. and Wade, J.D. (2017) Chem. Eur. J. 23, 390-396.
87. “Membrane insertion of a dinuclear polypyridylruthenium(II) complex revealed by solid-state NMR and molecular dynamics simulation – implications for selective antibacterial activity.” Weber, D., Sani, M.-A., Downton, M.T., Separovic, F., Keene, F.R. and Collins, J.G. (2016) J. Am. Chem. Soc. 138, 15267-15277.
88. “Total chemical synthesis of an intra-A-chain cystathionine human insulin analogue with enhanced thermal stability.” Karas, J.A., Patil, N.A., Tailhades, J. Sani, M.-A., Scanlon, D.B., Forbes, B.E., Gardiner, J., Separovic, F., Wade J.D., and Hossain, M.A. (2016) Angew. Chem. Int. Ed. 55, 14743-14747.
89. “Antimicrobial peptides share a common interaction driven by membrane line tension reduction.” Henderson, J.M., Waring, A.J., Separovic, F. and Lee, K.Y.C. (2016) Biophys. J. 111, 2176-2189.
90. “Interaction of the antimicrobial peptides caerin 1.1 and aurein 1.2 with intact bacteria by 2H solid-state NMR.” Laadhari, M., Arnold, A.A., Gravel, A.E., Separovic, F. and Marcotte, I. (2016) Biochim. Biophys. Acts 1858, 2959-2964.
91. “Activity and conformation of lysozyme in molecular solvents, protic ionic liquids (PILs) and salt-water systems.” Wijaya, E.C., Separovic, F., Drummond, C.J. and Greaves, T.L. (2016) Phys. Chem. Chem. Phys. 18, 25926-25936.
92. “Micelle formation of a non-ionic surfactant in non-aqueous molecular solvents and protic ionic liquids (PILs).” Wijaya, E.C., Separovic, F., Drummond, C.J. and Greaves, T.L. (2016) Phys. Chem. Chem. Phys. 18, 24377-24386.
93. “A one-pot chemically cleavable bis-linker tether strategy for the synthesis of heterodimeric peptides.” Patil, N.A., Tailhades, J., Karas, J., Separovic, F., Wade, J.D. and Hossain, M.A. (2016) Angew. Chem. Int. Ed. 55, 14552-14556,
94. “Exploring the structural relationship between encapsulated antimicrobial peptides and the bilayer membrane mimetic lipidic cubic phase: Studies with gramicidin A’.” Meikle, T.G., Conn, C.E., Separovic, F. and Drummond, C. (2016) RSC Adv. 6, 68685-68694.
95. “How membrane-active peptides get into lipid membranes.” Sani, M.-A. and Separovic, F.(2016) Acc. Chem. Res. 49, 1130-1138.
96. “Amyloid beta (Aβ) peptide and factors that play important roles in Alzheimer’s disease.” Jamasbi, E., Wade, J.D., Separovic, F. and Hossain, M.A. (2016) Curr. Med. Chem. 23, 884-892.
97. “Atomic force microscopy of bacteria reveals the mechanobiology of pore forming peptide action.” Mularski, A., Wilksch, J.J., Hanssen, E., Strugnell, R.A. and Separovic, F. (2016) Biochim. Biophys. Acta 1858, 1091-1098.
98. “Membrane interactions of proline-rich antimicrobial peptide, Chex1-Arg20, multimers.” Li, W., Sani, M.-A., Jamasbi, E., Otvos Jr, L., Hossain, M.A., Wade, J.D. and Separovic, F. (2016) Biochim. Biophys. Acta 1858, 1236-1243.
99. “Engineering of a novel simplified human insulin-like peptide 5 agonist.” Patil, N.A., Hughes, R.A., Rosengren, K.J., Kocan, M., Ang, S.Y., Tailhades, J., Separovic, F., Summers, R., Grosse, J., Wade, J.D., Bathgate, R.A.D. and Hossain, M.A. (2016) J. Med. Chem. 59, 2118-2125.
100. “Hypercrosslinked additives for ageless gas separation membranes.” Lau, C.H., Mulet, X., Konstas, K., Doherty, C.M., Sani, M.-A., Separovic, F., Hill, M.R. and Wood, C.D. (2016) Angew. Chem. Int. Ed. 55, 1998-2001.
101. “The C-terminus of the B-chain of human insulin-like peptide 5 is critical for cognate RXFP4 receptor activity.” Patil, N.A., Bathgate, R.A.D., Kocan, M., Ang, S.Y. Tailhades, J., Separovic, F., Summers, R., Grosse, J., Hughes, R.A., Wade, J.D. and Hossain, M.A. (2016) Amino Acids 48, 987-992.
102. “Model membrane and cell studies of antimicrobial activity of melittin analogues.” Jamasbi, E., Mularski, A. and Separovic, F. (2016) Curr. Top. Med. Chem. 16, 40-45.
103. “Membrane accessibility of glutathione.” Garcia, A., Eljack, N.D., Sani, M.-A., Separovic, F., Rasmussen, H.H., Khandelia, H., Cornelius, F. and Clarke, R.J. (2015) Biochim. Biophys. Acta 1848, 2430-2436.
104. “Multimerization of a designed proline-rich antimicrobial peptide, Chex-Arg20, alters the mechanism of its interaction with the Escherichia coli cell membrane.” Li, W., O’Brien-Simpson, N.M., Tailhades, J., Pantarat, N., Dawson, R.M., Otvos, L., Reynolds, E.C., Separovic, F., Hossain, M.A, and Wade, J.D. (2015) Chem. Biol. 22, 1250-1258.
105. “The prototypic cyclotide kalata B1 has a unique mechanism of entering cells.” Henriques, S.T, Huang, Y.-H., Chaousis, S., Sani, M.-A., Poth, A.G., Separovic, F. and Craik, D.J. (2015) Chem. Biol. 22, 1087-1097.
106. “Bacteria may cope differently from similar membrane damage caused by the Australian tree frog antimicrobial peptide maculatin 1.1.” Sani, M.-A., Henriques, S.T., Weber D. and Separovic, F. (2015) J. Biol. Chem. 290, 19853-19862.
107. “Proline-15 creates an amphipathic wedge in maculatin 1.1 peptides that drives lipid membrane disruption.” Sani, M.-A., Lee, T.-H., Aguilar, M.-I. and Separovic, F. (2015) Biochim. Biophys. Acta 1848, 2277-2289.
108. “Site of fluorescent label modifies interaction of melittin with live cells and model membranes.” Jamasbi, E., Ciccotosto, G.D., Tailhades, J., Robins-Browne, R.M., Ugalde, C.L., Sharples, R.A., Patil, N., Wade, J.D., Hossain, M.A. and Separovic, F. (2015) Biochim. Biophys. Acta 1848, 2031-2039.
109. “C-terminal modifications broaden activity of the proline-rich antimicrobial peptide, Chex1-Arg20.” Li, W., Tailhades, J., Hossain, M.A., O’Brien-Simpson, N.M., Reynolds, E.C., Otvos Jr, L., Separovic, F. and Wade, J.D. (2015) Aust. J. Chem. 68, 1373-1378.
110. “Atomic force microscopy reveals the mechanobiology of lytic peptide action on bacteria.” Mularski, A., Wilksch, J.J., Wang, H., Hossain, M.A., Wade, J.D., Separovic, F. Strugnell, R.A. and Gee, M.L. (2015) Langmuir 31, 6164-6171.
111. “Characterization of lipid-binding site of equinatoxin II by NMR and molecular dynamics simulation.” Weber, D.K., Yao, S., Rojko, N., Anderluh, G., Lybrand, T.P., Downton, M.T., Wagner, J. and Separovic, F. (2015) Biophys. J. 108, 1987-1996.
112. “Progression of NMR studies of membrane-active peptides from lipid bilayers to live cells.” Sani, M.-A. and Separovic, F. (2015) J. Magn. Reson. 253, 138-142.
113. “Subtle differences in initial membrane interactions underpin selectivity of small antimicrobial peptides.” Praporski, S., Mechler, A., Separovic, F. and Martin, L.L. (2015) ChemPlusChem 80, 91-96.
114. “Synthetic covalently linked dimeric form of H2 relaxin retains native RXFP1 activity and has improved in vitro serum stability.” Nair, V.B., Bathgate, R.A.D., Separovic, F., Samuel, C.S., Hossain, M.A. and Wade, J.D. (2015) BioMed Res. Int. 2015, article ID 731852, 9 pages.
115. “Cellular disulfide bond formation in bioactive peptides and proteins.” Patil, N., Tailhades, J., Separovic, F., Hughes, R.A., Wade, J.D. and Hossain, M.A. (2015) Int. J. Mol. Sci. 16, 1791-1805.
116. “Melittin peptides exhibit different activity on different cells and model membranes.” Jamasbi, E., Batinovic, S., Sharples, R.A., Sani, M.-A., Robins-Browne, R.M., Wade, J.D., Separovic, F. and Hossain, M.A. (2014) Amino Acids 46, 2759-2766.
117. “Proline-rich antimicrobial peptides: multiple potential therapeutics against antibiotic resistant bacteria.” Li, W., Tailhades, J., O’Brien-Simpson, N.M., Hossain, M.A., Separovic, F. and Wade, J.D. (2014) Amino Acids 46, 2287-2294.
118. “Dye-release assay for investigation of antimicrobial peptide activity in a competitive lipid environment.” Sani, M.-A., Gagne, E., Gehman, J.D., Whitwell, T.C. and Separovic, F. (2014) Eur. Biophys. J. 43, 445-450.
119. “2-Nitroveratryl as a photocleavable thiol protecting group for directed disulfide bond formation in the chemical synthesis of insulin.” Karas, J.A., Scanlon, D.B., Forbes, B.E., Vetter, I., Lewis, R.J., Gardiner, J., Separovic, F., Wade, J.D. and Hossain, M.A. (2014) Chem. Eur. J. 20, 9549-9552.
120. “Measuring translational diffusion coefficients of peptides and proteins by PFG-NMR using band-selective RF pulses.” Yao, S., Weber, D.K., Separovic, F. and Keizer, D.W. (2014) Eur. Biophys. J. 43, 331-339.
121. “Comparison of reversible membrane destabilisation induced by antimicrobial peptides derived from Australian frogs.” Lee, T.-H., Heng, C., Separovic, F. and Aguilar, M.-I. (2014) Biochim. Biophys. Acta 1838, 2205-2215.
122. “Membrane interactions and biological activity of antimicrobial peptides from Australian scorpion.” Luna-Ramírez, K., Sani, M.-A., Silva-Sanchez, J., Jiménez-Vargas, J.M., Reyna-Flores, F., Winkel, K.D., Wright, C.E., Possani, L.D. and Separovic, F. (2014) Biochim. Biophys. Acta 1838, 2140-2148.
123. “The investigation of membrane binding by amphibian peptide agonists of CCK2R using 31P and 2H solid-state NMR.” Sherman, P.J., Separovic, F. and Bowie, J.H. (2014) Peptides 55, 98-102.
124. “Solid-state NMR studies of antimicrobial peptide interactions with specific lipid environments.” Sani, M.-A. and Separovic, F. (2014) in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides. eds. F. Separovic and A. Naito, RSC Books, London, U.K., Chapter 15, pp287-303.
125. “Preface.” Separovic, F. and Naito, A. (2014) in Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides. eds. F. Separovic and A. Naito, RSC Books, London, U.K., P005-P006.
126. “Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides.” eds. Separovic, F. and Naito, A. (2014) RSC Books, London, U.K., pp 608.
127. “Cyclization enhances function of linear anti-arthritic peptides.” Ali, M., Amon, M., Bender, V., Bolte, A., Separovic, F., Benson, H. and Manolios, N. (2014) Clin. Immunol. 150, 121-133.
128. “Synthesis of fluorescent analogues of relaxin family peptides and their preliminary in vitro and in vivo characterization.” Chan, L.J., Smith, C.M., Chua, B.E., Lin, F., Bathgate, R.A.D., Separovic, F., Gundlach, A.L., Hossain, M.A. and Wade, J.D. (2013) Frontiers Chem. 1, article 30, 9 pages.
129. “Total chemical synthesis of a heterodimeric interchain bis-lactam-linked peptide: application to an analogue of human insulin-like peptide 3.” Karas, J., Shabanpoor, F. Hossain, M.A., Gardiner, J., Separovic, F., Wade, J.D. and Scanlon, D.B. (2013) Int. J. Peptides 2013, article ID 504260, 8 pages.
130. “Relaxin and its role in fibrotic diseases.” Chan, L.J., Samuel, C.S., Separovic, F., Hossain, M.A. and Wade, J.D. (2013) Amino Acids, Pept. Proteins 38, 60–78.
131. “Controlling nanostructure and lattice parameter of the inverse bicontinuous cubic phases in functionalised phytantriol dispersions.” Fraser, S.J., Mulet, X., Hawley, A., Separovic, F. and Polyzos, A. (2013) J. Colloid Interface Sci. 408, 117-124.
132. “Maculatin 1.1 disrupts S. aureus lipid membranes via a pore mechanism.” Sani, M.-A., Whitwell, T.C., Gehman, J.D., Robins-Browne, R.M., Pantarat, N., Attard, T.J., Reynolds E.C., O’Brien-Simpson, N.M. and Separovic, F. (2013) Antimicrob. Agents Chemother. 57, 3593-3600.
133. “Membrane defects enhance the interaction of antimicrobial peptides, aurein 1.2 versus caerin 1.1.” Fernandez, D.I., Sani, M.-A., Miles, A.J., Wallace, B.A. and Separovic, F. (2013) Biochim. Biophys. Acta 1828, 1863-1872.
134. “A practical implementation of de-Pake-ing via weighted Fourier transformation.” Sani, M.-A., Weber, D.K., Delaglio, F., Separovic, F. and Gehman, J.D. (2013) PeerJ 1:e30 http://dx.doi.org/10.7717/peerj.30 .
135. “Proline facilitates the membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disordering.” Fernandez, D.I., Lee, T.-H., Sani, M.-A., Aguilar, M.-I. and Separovic, F. (2013) Biophys. J. 104, 1495-1507.
136. “The importance of tryptophan B28 in H2 relaxin for RXPF2 binding and activation.” Chan, L.J., Wade, J.D., Separovic, F., Bathgate, R.A.D. and Hossain, M.A. (2013) Int. J. Pept. Res. Ther. 19, 55-60.
137. “Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers.” Fernandez, D.I., Le Brun, A.P., Lee, T.-Z., Bansal, P., Aguilar, M.-I., James, M. and Separovic, F. (2013) Eur. Biophys. J. 42, 47-59.
138. “The antimicrobial peptide aurein 1.2 disrupts model membranes via the carpet mechanism.” Fernandez, D.I., Le Brun, A.P., Whitwell, T.C., Sani, M.-A., James, M. and Separovic, F. (2012) Phys. Chem. Chem. Phys. 14, 15739-15751.
139. “Identification of key residues essential for the structural fold and receptor selectivity within the A-chain of H2 relaxin.” Chan, L.J., Rosengren, K.J., Layfield, S.L., Bathgate, R.A.D., Separovic, F., Samuel, C.S., Hossain, M.A. and Wade, J.D. (2012) J. Biol. Chem. 287, 41152-41164.
140. “Human relaxin-2: historical perspectives and role in cancer biology.” Nair, V.B., Samuel, C.S., Separovic, F., Hossain, M.A. and Wade, J.D. (2012) Amino Acids 43, 1131-1140.
141. “Electrochemistry of room temperature protic ionic liquids: a critical assessment for use as electrolytes in electrochemical applications.” Lu, X., Burrell, G., Separovic, F. and Zhao, C. (2012) J. Phys. Chem. B 116, 9160-9170.
142. “Host-defense peptides of Australian anurans. Part 2. Structure, mechanism of action, and evolutionary significance.” Bowie, J.H., Separovic, F. and Tyler, M.J. (2012) Peptides 37, 174-188.
143. “The lipid network.” Sani, M.-A., Separovic, F. and Gehman, J.D. (2012) Biophysical Rev. 4, 283-290.
144. “Copper modulation of amyloid beta 42 interactions with model membranes.” Weber, D.K., Gehman, J.D., Separovic, F. and Sani, M.-A. (2012) Aust. J. Chem. 65, 472-479.
145. “Minimization of human relaxin-3 leading to high affinity analogues with increased selectivity for relaxin-family peptide 3 receptor RXFP3 over RXFP1.” Shabanpoor, F., Hossain. M.A., Ryan, P.J., Belgi, A., Layfield, S., Kocan, M., Zhang, S, Samuel, C.S., Gundlach, A.L., Bathgate, R.A.D., Separovic, F. and Wade, J.D. (2012) J. Med. Chem. 55, 1671-1681.
146. “Surface immobilization of bio-functionalized cubosomes: sensing of proteins by quartz crystal microbalance.” Fraser, S.J., Mulet, X., Martin, L., Praporski, S., Mechler, A., Hartley, P.G., Polyzos, A. and Separovic, F. (2012) Langmuir 28, 620-627.
147. “Lipid composition regulates the conformation and insertion of the antimicrobial peptide maculatin 1.1.” Sani, M.-A., Whitwell, T.C. and Separovic, F. (2012) Biochim. Biophys. Acta 1818, 205-211.
148. “Membrane protein structure and function.” (preface) Allen, T.W. and Separovic, F. (2012) Biochim. Biophys. Acta 1818, 125.
149. “Solid-state NMR of amyloid membrane interactions.” Gehman, J.D. and Separovic, F. (2011) in Protein Folding, Misfolding, and Disease, eds. A.F Hill, R. Cappai, K. Barnham and S.P. Bottomley, Humana Press, New York, USA, Chapter 11, pp 165-177; Methods Mol. Biol. 752, 165-77.
150. “Preparation and biological evaluation of self-assembled cubic phases for the polyvalent inhibition of cholera toxin.” Fraser, S.J., Rose, R., Hattarki, M.K., Hartley, P.G., Dolezal, O., Dawson, R.M., Separovic, F. and Polyzos, A. (2011) Soft Matter 7, 6125-6134.
151. “Interactions of the antimicrobial peptide maculatin 1.1 and analogues with phospholipid bilayers.” Fernandez, D.I., Sani, M.-A. and Separovic, F. (2011) Aust. J. Chem. 64, 798-805.
152. “Modeling the membrane environment for membrane proteins.” Separovic, F., Killian, J.A., Cotton, M., Busath, D.D. and Cross, T.A. (2011) Biophys. J. 100, 2073-2074.
153. “Disentanglement of heterogeneous dynamics in mixed lipid systems.” Sani, M.-A., Separovic, F. and Gehman, J.D. (2011) Biophys. J. 100, L40-L42.
154. “Interactions of a synthetic Leu-Lys rich antimicrobial peptide with phospholipid bilayers.” Fernandez, D.I., Sani, M.-A., Gehman, J.D, Hahm, K.-S. and Separovic, F. (2011) Eur. Biophys. J. 40, 471-480.
155. “QCM-D fingerprinting of membrane-active peptides.” McCubbin, G.A., Praporski, S., Piantavigna, S., Knappe, D., Hoffman, R. Bowie, J.H., Separovic, F. and Martin, L.L. (2011) Eur. Biophys. J. 40, 437-446.
156. “Special Issue on Membrane Active Peptides.” (preface) Afonin, S., Juretic, D., Separovic, F. and Ulrich, A. (2011) Eur. Biophys. J. 40, 347-348.
157. “The relaxin peptide family — structure, function and clinical applications.” Chan, L.J., Hossain, M.A., Samuel, C.S., Separovic, F. and Wade, J.D. (2011) Protein and Peptide Letters 18, 220-229.
158. “Lipid matrix plays a role in Abeta fibril kinetics and morphology.” Sani, M.-A., Gehman, J.D. and Separovic, F. (2011) FEBS Lett. 585, 749-754.
159. “General method for selective labelling of double-chain cysteine-rich peptides with a lanthanide chelate via solid-phase synthesis.” Shabanpoor, F., Separovic, F. and Wade, J.D. (2011) J. Pept. Sci. 17, 169-173.
160. “Design and development of analogues of dimers of insulin-like peptide 3 (INSL3)B-chain as high affinity antagonists of RXFP2.” Shabanpoor, F., Zhang, S., Hughes, R.A., Hossain, M.A., Layfield, S., Ferraro, T., Bathgate, R.A.D., Separovic, F. and Wade, J.D. (2011) Biopolymers Peptide Science 96, 81-87.
161. “Solid-state NMR of membrane-acting antimicrobial peptides.” Gehman, J.D., Sani, M.A and Separovic, F. (2011) in Biomolecular NMR Spectroscopy, eds. A. Dingley and S. Pascal, IOS Press, Amsterdam, The Netherlands, Chapter 8, pp 137-161.
162. “Development of cubosomes as a cell-free biosensing platform.” Fraser, S.J., Dawson, R.M., Waddington, L.J., Muir, B.W., Mulet, X., Hartley, P.G., Separovic, F. and Polyzos, A. (2011) Aust. J. Chem. 64, 46-53.
163. “Stereospecific interactions are necessary for Alzheimer disease amyloid-β toxicity.” Ciccotosto, G.D., Tew, D.J., Drew, S.C., Smith, D.G., Johanssen, T., Lal, V., Lau, T.-L., Perez, K., Curtain, C., Wade, J.D., Separovic, F., Masters, C.L., Smith, J.P., Barnham, K.J. and Cappai, R. (2011) Neurobiology of Aging 32, 235-248.
164. “NMR relaxation and self-diffusion study at high and low magnetic fields of ionic association in protic ionic liquids.” Burrell, G.L., Burgar, I.M., Gong, Q., Dunlop, N.F. and Separovic, F. (2010) J. Phys. Chem. B 114, 11436-11443.
165. “Anionic phospholipid interactions of the prion protein N terminus are minimally perturbing and not driven solely by the octapeptide repeat domain.” Boland, M.P., Hatty, C.R., Separovic, F., Hill, A.F., Tew, D.J., Barnham, K.J., Haigh, C.L., James, M., Masters, C.L. and Collins, S.J. (2010) J. Biol. Chem. 285, 32282-32292.
166. “Real time quantitative analysis of lipid disordering by aurein 1.2 during membrane adsorption, destabilisation and lysis.” Lee, T.-Z., Heng, C., Swann, M.J., Gehman, J.D., Separovic, F., Aguilar, M.-I. (2010) Biochim. Biophys. Acta 1798, 1977-1986.
167. “Self assembly of spherical peptide nanoparticles for delivery of hydrophilic moieties to the cytosol.” Collins, L., Parker, A.L., Gehman, J., Eckley, L., Perugini, M.A., Separovic, F. and Fabre, J.W. (2010) ACS Nano 4, 2856-2864.
168. “Non-Newtonian viscous shear-thinning in ionic liquids.” Burrell, G.F., Dunlop, N.F. and Separovic, F. (2010) Soft Matter 6, 2080-286.
169. “Preparation of protic ionic liquids with minimal water content and 15N NMR study of proton transfer.” Burrell, G.L., Burgar, I.M., Separovic, F. and Dunlop, N.F. (2010) Phys. Chem. Chem. Phys. 12, 1571-1577.
170. “Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.” Lam, Y.H., Hung, A., Norton, R.S., Separovic, F., and Watts, A. (2010) Proteins 78, 858-872.
171. “Design, synthesis and in vitro pharmacological characterization of novel improved high affinity INSL3 antagonists.” Shabanpoor, F., Hughes, R.A., Zhang, S., Bathgate, R.D., Layfield, S., Hossain. M.A., Tregear, G.W., Separovic, F. and Wade, J.D. (2010) Amino Acids 38, 121-131.
172. “Solid-state NMR study of membrane interactions of the pore-forming cytolysin, equinatoxin II.” Drechsler, A., Anderluh, G., Norton, R.S. and Separovic, F. (2010) Biochim. Biophys. Acta 1798, 244-251.
173. “The solution structure and membrane interactions of the antimicrobial peptide fallaxidin 4.1a: an NMR and QCM study.” Sherman, P., Jackway, R., Gehman, J., Praporski, S., McCubbin, G., Mechler, A., Martin, L., Separovic, F. and Bowie, J. (2009) Biochemistry 48, 11892-11901.
174. “Development of lanthanide-labelled human INSL3 as an alternative probe to radioactively-labelled INSL3 for use in bioassays.” Shabanpoor, F., Hughes, R.A., Bathgate, R.A.D., Separovic, F. and Wade J.D. (2009) in Relaxin and Related Peptides: Fifth International Conference, eds. G.D. Bryant-Greenwood, C.A. Bagnell and R.A.D. Bathgate, Ann. NY Acad. Sci. 1160, 87-90.
175. “Cubic phases of ternary amphiphile-water systems.” Fraser, S., Separovic, F. and Polyzos, A. (2009) Eur. Biophys. J. 39, 83-90.
176. “The chemistry and biology of insulin-like peptide 3, a novel member of the insulin superfamily.” Shabanpoor, F., Hughes, R.A., Separovic, F. and Wade, J.D. (2009) in Bioactive Peptides, eds. J. Howl and S. Jones, Taylor and Francis Inc., Abingdon UK, Chapter 7, pp 159-168.
177. “Host defence peptides from the secretion of the skin glands of frogs: membrane active peptides from the genera Litoria, Uperoleia and Crinia.” Bowie, J.H., Jackway, R.J., Separovic, F., Carver, J.A., and Tyler, M.J. (2009) in Bioactive Peptides, eds. J. Howl and S. Jones, Taylor and Francis, Inc., Abingdon UK, Chapter 15, pp 333-355.
178. “Effect of lipid on the conformation of the N-terminal region of equinatoxin II: a synchrotron radiation CD study.” Drechsler, A., Miles, A.J., Norton, R.S., Wallace, B.A. and Separovic, F. (2009) Eur. Biophys. J. 39, 121-127.
179. “The human insulin superfamily of polypeptide hormones.” Shabanapoor, F., Separovic, F. and Wade, J.D. (2009) in Vitamins and Hormones — Vol. 80, ed. G. Litwack, Elsevier, The Netherlands: pp1-31.
180. “Membrane interactions of antimicrobial peptides from Australian frogs.” Fernandez, D.I., Gehman, J.D. and Separovic, F. (2009) Biochim. Biophys. Acta 1788, 1630-1638.
181. “Physico-chemical characterization of structure and stability of rifampicin liposome dry powders for inhalation.” Changsan, N., Chan, H.-K., Separovic, F. and Srichana, T. (2009) J. Pharmaceut. Sci. 98, 628-639.
182. “Determination of rifampicin location in cholesterol-lipid liposomes by 2H and 31P solid-state NMR.” Changsan, N., Separovic, F. and Srichana, T. (2008) 2nd IEEE International Nanoelectronics Conference, INEC 2008, art. no. 4585514, pp. 397-401.
183. “The effects of lipids on the structure of the eukaryotic cytolysin equinatoxin II: a synchrotron radiation circular dichroism spectroscopic study.” Miles, A.J., Drechsler, A., Kristan, K., Anderluh, G., Norton, R.S., Wallace, B.A. and Separovic, F. (2008) Biochim. Biophys. Acta 1778, 2091-2096.
184. “Effect of antimicrobial peptides from Australian tree frogs on anionic phospholipid membranes.” Gehman, J.D., Luc, F., Hall, K., Lee, T.-H., Boland, M.P., Pukala, T.L., Bowie, J.H., Aguilar, M.I. and Separovic, F. (2008) Biochemistry 47, 8557-8565.
185. “Solid-phase synthesis of europium-labelled human INSL3 as a novel probe for the study of ligand-receptor interactions.” Shabanpoor, F., Hughes, R.A., Bathgate, R.A.D., Zhang, S., Scanlon, D.B., Hossain, M.A., Separovic, F. and Wade, J.D. (2008) Bioconjugate Chem. 19, 1456-1463.
186. “A solid-state NMR study of the interaction of fish antifreeze proteins with phospholipid membranes.” Garner, J., Inglis, S.I., Hook, J., Separovic, F. and Harding, M.M. (2008) Eur. Biophys. J. 37, 1031-1038.
187. “Electrochemistry in room temperature protic ionic liquids.” Zhao, C., Burrell, G., Torriero, A.A.J., Separovic, F., Dunlop, N.F., MacFarlane, D.R. and Bond, A.M. (2008) J. Phys. Chem. B. 112, 6923-6936.
188. “Metal effects on the membrane interactions of amyloid-β peptides.” Gehman, J.D., O”Brien, C.C., Shabanpoor, F., Wade, J.D. and Separovic, F. (2008) Eur. Biophys. J. 37, 333-344.
189. “Metals and Membranes in Neuroscience.” (preface) Curtain, C. and Separovic, F. (2008) Eur. Biophys. J. 37, p239.
190. “Liposomal phospholipid preparations of chloramphenicol for ophthalmic applications.” Mahmoud, S.S., Gehman, J.D., Azzopardi, K., Robins-Browne, R.M. and Separovic, F. (2008) J. Pharmaceutical Sci. 97, 2691-2701.
191. “Cholesterol and Clioquinol modulation of Aβ(1-42) interaction with phospholipid bilayers and metals” Lau, T.-L., Gehman, J.D., Wade, J.D., Masters, C.L., Barnham, K.J. and Separovic, F. (2007) Biochim. Biophys. Acta 1768, 3135-3144.
192. “International trend in biophysics — The Australian Society for Biophysics: a brief history.” Norton, R. and Separovic, F. (2007) Seibutsu Butsuri 47, 338-340.
193. “Specific and selective peptide-membrane interactions revealed using quartz crystal microbalance.” Mechler, A., Praporski, S., Atmuri, K., Boland, M., Separovic, F. and Martin, L.L. (2007) Biophys. J. 93, 3907-3916.
194. “Characterization of extracellular polysaccharides produced by the fungus Acremonium.” Schmid, F., Separovic, F., McDougall, B.M., Stone, B.A., Brownlee, R.T.C. and Seviour, R.J. (2007) Carbohydrate Res. 342, 2481-2483.
195. “From physics to biology.” (book review). Gehman, J. and Separovic, F. (2007) Australian Physics April/May 2007, p30.
196. “Interactions of the Australian tree frog antimicrobial peptides aurein 1.2, citropin 1.1 and maculatin 1.1 with lipid model membranes: differential scanning calorimetric and Fourier transform infrared spectroscopic studies.” Seto, G.W.J., Marwaha, S., Kobewka, D.M., Lewis, R.N.A.H., Separovic, F. and McElhaney, R.N. (2007) Biochim. Biophys. Acta. 1768, 2787-2800.
197. “Membrane interactions and the effect of metal ions on the amyloidogenic fragment Aβ(25-35) in comparison to Aβ(1-42).” Lau, T.-L., Gehman, J.D., Wade, J.D., Perez, K., Masters, C.L., Barnham, K.J. and Separovic, F. (2007) Biochim. Biophys. Acta 1768, 2400-2408.
198. “Boltzmann statistics rotational-echo double resonance-analysis.” Gehman, J.D., Separovic, F., Lu, K. and Mehta, A.K. (2007) J. Phys. Chem. B. 111, 7802-7811.
199. “The conformation of acetylated virginiamycin M1 and virginiamycin M1 in explicit solvents.” Ng, C. A., Zhao, W., Dang, J., Bergdahl, M., Separovic, F., Brownlee R.T.C. and Metzger, R.P. (2007) Biochim. Biophys. Acta 1774, 610-618.
200. “β-sheet structured β-amyloid(1-40) perturbs phosphatidylcholine model membranes.” de Planque, M.R.R., Raussens, V., Contera, S.A., Rijkers, D.T.S., Liskamp, R.M.J., Ruysschaert, J.-M., Ryan, J.F., Separovic, F. and Watts, A. (2007) J. Mol. Biol. 368, 982 -987.
201. “Cupiennin 1a, an antimicrobial peptide from the venom of the neotropical wandering spider Cupiennius salei, also inhibits the formation of nitric oxide by neuronal nitric oxide synthase.” Pukala, T.L., Doyle, J.R., Llewellyn, L.E., Kuhn-Nentwig, L., Separovic, F. and Bowie, J.H. (2007) FEBS J. 274, 1778-1785.
202. “Solution structure and interaction of cupiennin 1a, a spider venom peptide, with phospholipid bilayers.” Pukala, T.L., Boland, M.P., Gehman, J.D., Kuhn-Nentwig, L., Separovic, F. and Bowie, J.H. (2007) Biochemistry 46, 3576-3585.
203. “Selective permeabilization of the host cell membrane of Plasmodium falciparum-infected red blood cells by streptolysin O and equinatoxin II.” Jackson, K.E., Spielmann, T., Hanssen, E., Adisa, A., Separovic, F., Dixon, M.W.A., Trenholme, K.R., Hawthorne, P.L., Gardiner, D.L., Gilberger, T. and Tilley, L. (2007) Biochem. J. 403, 167-175.
204. “Gated ion channel based biosensor device.” Separovic, F. and Cornell, B.A. (2007) in Biological Membrane Ion Channels: Dynamics, Structure and Applications (S.H. Chung, O.S. Andersen and V. Krishnamurthy, eds.) Springer, New York, U.S.A. pp 595-621.
205. “39K NMR of free potassium in geopolymers.” Duxson, P., Provis, J.L., Lukey, G.C., van Deventer, J.S.J., Separovic, F. and Gan, Z.H. (2006) Ind. Eng. Chem. Res. 45, 9208-9210.
206. “Copper mediated amyloid-b toxicity is associated with an intermolecular histidine bridge.” Smith, D.P., Smith, D.G., Curtain, C.C., Boas, J.F., Pilbrow, J.R., Ciccotosto, G.D., Lau, T.-L., Tew, D.J., Perez, K., Wade, J.D., Bush, A.I., Drew, S.C., Separovic, F., Masters, C.L., Cappai, R. and Barnham, K.J. (2006) J. Biol. Chem. 281, 15145-15154.
207. “Membrane interactions of antimicrobial peptides from Australian tree frogs.” Boland, M.P. and Separovic, F. (2006) Biochim. Biophys. Acta 1758, 1178-1183.
208. “Effect of linker length on avidin binding to biotinylated gramicidin A.” Anastasiadis, A., Morton, C.J., Talbo, G.H., Koeppe II, R.E. and Separovic, F. (2006) Intl J. Peptide Res. Therap. 12, 243-252.
209. “Orientational order of Australian spider silks as determined by solid state NMR.” Bonev, B., Grieve, S., Herberstein, M.E., Kishore, A.I., Watts, A. and Separovic, F. (2006) Biopolymers 82, 134-143.
210. “Copper and zinc mediated oligomerisation of Ab peptides.” Ali, F.E., Separovic, F., Barrow, C.J., Yao, S. and Barnham, K.J. (2006) Intl J. Peptide Res. Therap. 12, 153-164.
211. “Interfacial properties of the M1 segment of the nicotinic acetylcholine receptor.” Ambroggio, E.E., Villarreal, M.A., Montich, G.G., Rijkers, D.T.S., de Planque, M.R.R., Separovic, F. and Fidelio, G.D. (2006) Biophys. Chem. 121, 171-176.
212. “Structure and activity of the N-terminal region of the eukaryotic cytolysin equinatoxin II.” Drechsler, A., Potrich, C., Sabo, J., Frisanco, M., Guella, G., Dalla Serra, M., Anderluh, G., Separovic, F. and Norton, R.S. (2006) Biochemistry 45, 1818-1828.
213. “Amyloid-b peptide disruption of lipid membranes and the effect of metal ions.” Lau, T.-L., Ambroggio, E.E., Tew, D.J., Cappai, R., Masters, C.L., Fidelio, G.D., Barnham, K.J. and Separovic, F. (2006) J. Mol. Biol. 356, 759-770.
214. “Amino functionalisation of microemulsion templated mesoporous silica foams.” Boskovic, S., Separovic, F., Turney, T.W., Stevens, G.W., Gee, M.L. and O”Connor, A.J. (2006) in Studies in Surface Science and Catalysis (Characterisation of Porous Solids VII) Elsevier 160, 591-598.
215. “Dimerisation of N-acetyl-L-tyrosine ethyl ester and Ab peptides via formation of dityrosine.” Ali, F.E. Leung, A., Cherny, R., Mavros, C., Barnham, K.J., Separovic F. and Barrow, C.J. (2006) Free Radical Research 40, 1-9.
216. “Solid-state NMR of membrane-active proteins and peptides.” Gehman, J.D. and Separovic, F. (2006) in Modern Magnetic Resonance Part 1: Applications in Chemistry, Biological and Marine Sciences (T. Asakura, H. Saito and I. Ando, eds.) Springer, New York, U.S.A. pp 301-307.
217. “Modeling speciation in highly concentrated alkaline silicate solutions.” Provis, J.L., Duxson, P., Lukey, G.C., Separovic, F., Kriven, W.M. and van Deventer, J.S.J. (2005) Ind. Eng. Chem. Res. 44, 8899-8908.
218. “Direct visualization of membrane leakage induced by the antibiotic peptides: maculatin, citropin and aurein.” Ambroggio, E.E., Separovic, F., Bowie, J.H., Fidelio, G.D. and Bagatolli, L.A. (2005) Biophys. J. 89, 1874-1881.
219. “Post-synthesis vapour phase functionalisation of MCM-48 with hexamethyldisilazane and 3-aminopropyldimethylethoxylsilane for bioseparation application.” Daehler, A., Boskovic, S., Gee, M.L., Separovic, F., Stevens, G.W. and O’Connor, A.J. (2005) J. Phys. Chem. B. 109, 16263-16271.
220. “Surface behavior and lipid interaction of Alzheimer b-amyloid peptide 1-42: a membrane-disrupting peptide. Ambroggio, E.E., Kim, D.H., Separovic, F., Barrow, C.J., Barnham, K.J., Bagatolli, L.A. and Fidelio, G.D. (2005) Biophys. J. 88, 2706-2713.
221. “29Si NMR study of structural ordering in aluminosilicate geopolymer gels.” Duxson, P., Provis, J.L., Lukey, G.C., Separovic, F. and van Deventer, J.S.J. (2005) Langmuir 21, 3028-3036.
222. “Developments in hyphenated spectroscopic methods in natural product profiling.” Urban, S. and Separovic, F. (2005) in Frontiers in Drug Design and Discovery 1 (Atta-ur-Rahman, G. Caldwell, eds.) Bentham Science Publishers. pp 113-166.
223. “The role of Ab peptides in Alzheimer”s disease.” Tickler, A.K., Wade, J.D. and Separovic, F. (2005) Protein & Peptide Lett. 12, 513-519.
224. “The conformational flexibility of the antibiotic virginiamycin M1.” Dang, J., Metzger, R.P., Brownlee, R.T.C., Ng, C.A., Bergdahl, M. and Separovic, F. (2005) Eur. Biophys. J. 34, 383-388.
225. “Interaction of the eukaryotic pore-forming cytolysin equinatoxin II with model membranes: 19F NMR studies.” Anderluh, G., Razpotnik, A., Podlesek, Z., Macek, P., Separovic, F. and Norton, R.S. (2005) J. Mol. Biol. 347, 27-39.
226. “Matrix method for analysis of selective NMR pulses.” Tesiram, Y.A. and Separovic, F. (2005) Concepts in Magnetic Resonance 25A, 1-17.
227. “The effect of alkali cations on aluminium incorporation in geopolymeric gels.” Duxson, P., Lukey, G.C., Separovic, F. and van Deventer, J.S.J. (2005) Ind. Eng. Chem. Res. 44, 832-839.
228. “Methionine regulates copper/hydrogen peroxide oxidation products of Ab.” Ali, F.E. Separovic, F., Barrow, C.J., Cherny, R.A., Fraser, F., Bush, A.I., Masters, C.L. and Barnham, K.J. (2005) J. Peptide Science 11, 353-360.
229. “Solvent affects the conformation of virginiamycin M1 (pristinamycin IIA, streptogramin A).” Dang, J., Separovic, F., Bergdahl, M., Brownlee, R.T.C., and Metzger, R.P. (2004) Org. Biomol. Chem. 2, 2919-2924.
230. “The aM1 segment of the nicotinic acetylcholine receptor exhibits conformational flexibility in a membrane environment.” de Planque, M.R.R., Rijkers, D.T.S., Fletcher, J., Liskamp, R.M.J. and Separovic, F. (2004) Biochim. Biophys. Acta. 1665, 40-47.
231. “An introduction to biological solid state NMR.” Dodd, A. and Separovic, F. (2004) Supramolecular Structure and Function 8 (G. Pifat-Mrzljak, ed.) Kluwer Academic / Plenum Publishers, New York, U.S.A. pp 145-156.
232. “Surface behaviour and peptide-lipid interactions of the antibiotic peptides, maculatin and citropin.” Ambroggio, E.E., Separovic, F., Bowie, J. and Fidelio, G.D. (2004) Biophys. Biochim. Acta 1664, 31-37.
233. “Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.” Apponyi, M.A., Pukala, T.L., Brinkworth, C.S., Maselli, V.M., Bowie, J.H., Tyler, M.J., Booker, G.W., Wallace, J.C., Carver, J.A., Separovic, F., Doyle, J. and Llewellyn, L.E. (2004) Peptides 25, 1035-1054.
234. “Metal catalyzed oxidative damage and oligomerization of the amyloid-b peptide (Ab) of Alzheimer”s disease.” Ali, F.E., Barnham, K.J., Barrow, C.J. and Separovic, F. (2004) Aust. J. Chem. 57, 511-518.
235. “Difference in conformation of virginiamycin M1 in chloroform and bound form in the 50S ribosome or streptogramin acetyltransferase.” Dang, J., Bergdahl, B.M., Separovic, F., Brownlee, R.T.C. and Metzger, R.P. (2004) Aust. J. Chem. 57, 415-418.
236. “Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes” Balla, M.S., Bowie, J.H. and Separovic, F. (2004) Eur. Biophys. J. 33, 109-116.
237. “A multidimensional 1H NMR study of the effect of model membranes on the conformation of enkephalin.” Marcotte, I., Separovic, F., Gagn”, S.M. and Auger, M. (2004) Biophys. J. 86, 1587-1600.
238. “Magnetic moments: membrane protein structures by NMR.” Separovic, F., Drechsler, A. and Lau, T.L. (2004) Chemistry in Australia 71(1), 4-7.
239. “NMR structural elucidation of amino resins.” Angelatos, A.S., Burgar, M.I., Dunlop, N. and Separovic, F. (2004) J. Appl. Polymer Sci. 91, 3504-3512.
240. “The aM1 transmembrane segment of the nicotinic acetylcholine receptor interacts strongly with model membranes.” de Planque, M.R.R., Rijkers, D.T.S., Liskamp, R.M.J. and Separovic, F. (2004) Magn. Reson. Chem. 42, 148-154.
241. “Metal catalyzed oxidation of tyrosine residues by different oxidation systems of copper/hydrogen peroxide.” Ali, F.E., Barnham, K.J., Barrow, C.J. and Separovic, F. (2004) J. Inorg. Biochem. 98, 173-184.
242. “Copper catalysed oxidation of amino acids and Alzheimer”s disease.” Ali, F.E., Barnham, K.J., Barrow, C.J. and Separovic, F. (2003) Lett. Peptide Sci. 10, 405-412.
243. “Solid-state NMR structure determination.” Drechsler, A and Separovic, F. (2003) IUBMB Life 55, 515-523.
244. “Neurotoxic, redox-competent Alzheimer”s b-amyloid is released from lipid membrane by methionine oxidation.” Barnham, K.J., Ciccotosto, G.D., Tickler, A.K., Ali, F.E., Smith, D.G., Williamson, N.A., Lam, Y.-H., Carrington, D., Tew, D., Kocak, G., Volitakis, I., Separovic, F., Barrow, C.J, Wade, J.D., Masters, C.L., Cherny, R.A., Curtain, C.C., Bush, A.I., Cappai, R. (2003) J. Biol. Chem. 278, 42959-42965.
245. “Magnetic resonance studies of the b-amyloid peptide.” Lau, T.-L., Barnham, K.J., Curtain, C.C., Masters, C.L. and Separovic, F. (2003) Aust. J. Chem. 56, 349-356.
246. “Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide/lipid interactions.” de Planque, M.R.R., Bonev, B.B., Demmers, J.A.A., Greathouse, D.V., Koeppe II, R.E., Separovic, F., Watts, A. and Killian, J.A. (2003) Biochemistry 42, 5341-5348.
247. “Surface coating of MCM-48 via a gas phase reaction with hexamethyldisilazane (HMDS).” Daehler, A., Gee, M.L., Separovic, F., Stevens, G.W. and O”Connor, A.J. (2003) in Studies in Surface Science and Catalysis, v. 146 (Nanotechnology in Mesostructured Materials), Park, S.-E., Ryoo, R., Ahn, W.-S., Lee, C.W., Eds, Elsevier, Amsterdam 493-496.
248. “Solid-state NMR structural determination of components in an ion channel switch biosensor.” Anastasiadis, A. and Separovic, F. (2003) Aust. J. Chem. 56, 163-166.
249. “The aromaticity of ferrocene and some derivatives, ruthenocene and dibenzenechromium as determined via ring current assessment and 13C anisotropic contributions to the 1H NMR shielding.” Phillips, L., Separovic, F. and Aroney, M.J. (2003) New J. Chem. 27, 381-386.
250. “Effects of the eukaryotic pore-forming cytolysin equinatoxin II on lipid membranes and the role of sphingomyelin.” Bonev, B.B., Lam, Y.-H., Anderluh, G., Watts, A., Norton, R.S. and Separovic, F. (2003) Biophys. J. 84, 2382-2392.
251. “Interaction of antimicrobial peptides from Australian amphibians with lipid membranes.” Marcotte, I., Wegener, K.L., Lam, Y.-H., Chia, B.C.S., de Planque, M..R.R., Bowie, J.H., Auger, M. and Separovic, F. (2003) Chem. Phys. Lipids, 122, 107-120.
252. “Solid-state NMR relaxation studies of Australian spider silks.” Kishore, A.I., Herberstein, M.E., Craig, C.L. and Separovic, F. (2002) Biopolymers 61, 287-297.
253. “Solid-state NMR conformational studies of a melittin-inhibitor complex.” Lam, Y.-H., Morton, C.J. and Separovic, F. (2002) Eur. Biophys. J. 31, 383-388.
254. “A solid-state NMR study of protein mobility in lyophilised protein-sugar powders.” Lam, Y.-H., Bustami, R., Phan, T., Chan, H.-K. and Separovic, F. (2002) J. Pharm. Sci. 91, 943-951.
255. “Solid-state NMR spectroscopy: principles and applications.” (book review) Separovic, F. (2002) Chemistry in Australia 69(4), 27-28.
256. “Biophysical studies of transmembrane peptide derived from the T cell antigen receptor.” Ali, M., de Planque, M.R.R., Huynh, N., Manolios, N. and Separovic, F. (2002) Lett. Peptide Sci. 8, 227-233.
257. “Synthesis of deuterated aminocaproyl linkers.” Anastasiadis, A., Separovic, F. and White, J. (2001) Aust. J. Chem. 54, 747-750.
258. “A metallosupramolecular capsule with the topology of the tetrahedron, 33, assembled from four guanidine-based ligands and twelve cadmium centers.” Muller, I.M., Robson, R. and Separovic, F. (2001) Angewandte Chemie-International Ed. 40, 4385-4386.
259. “Solid-state NMR structure determination of melittin in a lipid environment.” Lam, Y.-H., Wassall, S.R., Morton, C.J., Smith, R. and Separovic, F. (2001) Biophys. J. 81, 2752-2761.
260. “A reexamination of the structure of ”honeycomb cadmium cyanide”.” Abrahams, B.F., Hoskins, B.F., Lam, Y.-H., Robson, R., Separovic, F. and Woodberry, P. (2001) J. Solid State Chem. 156, 51-56.
261. “Solid-state NMR study of ageing of colorbond polymer coating.” Separovic, F., Chau, H.-D. and Burgar, M.I. (2001) Polymer 42, 925-930.
262. “Conformational studies of a melittin-inhibitor complex.” Lam, Y.-H., Nguyen, V., Fakaris, E and Separovic, F. (2000) J. Protein Chem. 19, 529-534.
263. “Effect of avidin on channel kinetics of biotinylated gramicidin.” Rokitskaya, T.I., Antonenko, Y.N., Kotova, E.A., Anastasiadis, A. and Separovic, F. (2000) Biochemistry 39, 13053-13058.
264. “A 31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria.” Chia, B.C.S., Lam, Y.-H., Dyall-Smith, M., Separovic, F. and Bowie, J.H. (2000) Lett. Peptide Sc. 7, 151-156.
265. “Selective on-resonance irradiation of a dipolar doublet.” Separovic, F., Skrynnikov, N.R. and Sanctuary, B.C. (2000) Aust. J. Chem. 53, 351-361.
266. “Orientation dependence of NMR relaxation time, T1r, in lipid bilayers.” Separovic, F., Cornell, B. and Pace, R. (2000) Chem. Phys. Lipids 107, 159-167.
267. “Spatially resolved magnetic resonance.” (book review) Separovic, F. (1999) Adv. Mater. 11, 1396.
268. “Structure of peptide models of ion channels.” Separovic, F., Anastasiadis, A. and Lam, Y.-H. (1999) Australian Biochemist 30, 3-6.
269. “Gramicidin channel controversy — revisited.” Cross, T.A., Arseniev, A., Cornell, B.A., Davis, J.H., Killian, J.A., Koeppe II, R.E., Nicholson, L.K., Separovic, F. and Wallace, B.A. (1999) Nature Struct. Biol. 6, 610-611
270. “Determination of chemical shielding tensor of an indole carbon and application to tryptophan orientation of a membrane peptide.” Separovic, F., Ashida, J., Woolf, T., Smith, R. and Terao, T. (1999) Chem. Phys. Lett. 303, 493-498.
271. “NMR structure of C-terminally tagged gramicidin channels.” Separovic, F., Barker, S., Delahunty, M. and Smith, R. (1999) Biochim. Biophys. Acta 1416, 48-56.
272. “Variable-temperature one- and two-dimensional 13C CP/MAS NMR studies of the dynamics of monohaptocyclopentadienyl rings of hafnium and titanium tetracyclopentadienyl in the solid state.” Munson, E.J., Douskey, M.C., De Paul, S.M., Ziegeweid, M., Phillips. L., Separovic, F., Davies, M.S. and Aroney, M.J. (1999) J. Organometallic Chem. 577, 19-23.
273. “The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids.” Curtain, C., Separovic, F., Nielsen, K., Craik, D., Zhong, Y. and Kirkpatrick, A. (1999) Eur. Biophys. J. 28, 427-436.
274. “Optical modulation of the insertion of gramicidin channels into bilayer lipid membranes.” Osman, P., Martin, S., Milojevic, D., Tansey, C. and Separovic, F. (1998) Langmuir, 14, 4238-4242.
275. “A solid-state NMR study of protein hydration and stability.” Separovic, F., Lam, Y. H., Ke, X. and Chan, H.-K. (1998) Pharmaceutical Res. 15, 1816-21.
276. “Biological NMR spectroscopy.” (book review) Separovic, F. (1998) Concepts Magn. Reson. 10, 57-58.
277. “Sensitivity and NMR spectroscopy.” Separovic, F. (1996) Chemistry in Australia 63, 436-437.
278. “The effect of electric field on the NMR spectra of lipid dispersions.” Osman, P. and Separovic, F. (1996) The NMR Newsletter 452, 49-51.
279. “Effect of unsaturation on acyl chain order of phosphatidylcholines in a dioleoylphosphatidylethanolamine matrix.” Separovic, F. and Gawrisch, K. (1996) Biophys. J. 71, 274-282.
280. “NMR investigation of hydrocarbon chain packing in lipid bilayers of polyunsaturated phospholipids.” Holte, L.L., Separovic, F. and Gawrisch, K.G. (1996) Lipids 31, S-199-203.
281. “Membranes: carbon-13 NMR.” Separovic, F. and Cornell, B.A. (1996) Encyclopedia of Nuclear Magnetic Resonance, (Grant, D.M. and Harris, R.K. eds.) John Wiley, New York, Vol. 5, 3003-8.
282. “Sodium ion binding in the gramicidin A channel. Solid-state NMR studies of the tryptophan groups.” Separovic, F., Gehrmann, J., Milne, T., Cornell, B.A., Lin, S.Y. and Smith, R. (1994) Biophys. J. 67, 1495-1500.
283. “The amino-terminal region of the HIV-1 Nef protein is fusogenic.” Curtain, C.C., Separovic, F., Rivett, D., Kirkpatrick, A., Waring, A.J., Gordon, L.M., and Azad, A.A. (1994) AIDS Res. Human Retroviruses 10, 1231-1240.
284. “Structure and orientation of the pore-forming peptide, melittin, in lipid bilayers.” Smith, R., Separovic, F., Milne, T.J., Whittaker, A., Bennett, F.M., Cornell, B.A., and Makriyannis, A. (1994) J. Mol. Biol. 241, 456-466.
285. “Zeeman incremented multiple quantum NMR.” Bowden, G.J., Prandolini, M.J., Pope, J.M. and Separovic, F. (1993) J. Magn. Reson. 103A, 307-312.
286. “NMR order parameter analysis of a peptide plane aligned in a lyotropic liquid crystal.” Separovic, F., Pax,R. and Cornell, B. (1993) Molec. Phys. 78, 357–369.
287. “Melittin induced changes in lipid multilayers: a solid-state NMR study.” Smith, R., Separovic, F., Bennett, F.C. and Cornell, B.A. (1992) Biophys. J. 63, 469–474.
288. “C–13 chemical shift tensor of L–tryptophan and its application to polypeptide structure determination.” Separovic, F., Hayamizu, K., Smith, R. and Cornell, B.A. (1991) Chem. Phys. Lett. 181, 157–162.
289. “Actin dynamics studied by solid–state NMR spectroscopy.” Phillips, L., Separovic, F., Cornell, B.A., Barden, J.A. and dos Remedios, C.G. (1991) Eur. Biophys. J. 19, 147–155.
290. “Molecular sequence effect on the C–13 carbonyl chemical shift shielding tensor.” Separovic, F., Smith, R., Yannoni, C.S. and Cornell, B.A. (1990) J. Amer. Chem. Soc. 112, 8324–8328.
291. “Solid–state 13C NMR studies of the effects of sodium ions on the gramicidin A ion channel.” Smith, R., Thomas, D.E., Atkins, A., Separovic, F. and Cornell, B.A. (1990) Biochim. Biophys. Acta. 1026, 161–166.
292. “Tensorial sets for coupled pairs of spin 1/2 nuclei.” G.J. Bowden, J.P.D. Martin and Separovic, F. (1990) Molec. Phys. 70, 581–603.
293. “Localization of ubiquinone in membranes by NMR and neutron diffraction.” Cornell, B.A., Keniry, M.A., Knott, R., Post, A., Robertson, R., Separovic, F., Weir, L.E. and Westerman, P.W. (1990) in Highlights in Ubiquinone Research. G.Lenaz, O. Barnabei, A. Rabbi and M. Battino (eds.), Taylor & Francis: London, pp27–32.
294. “Effect of acyl chain length on the structure and motion of gramicidin A in lipid bilayers.” Cornell, B.A., Separovic, F., Thomas, D.E., Atkins, A.R. and Smith, R. (1989) Biochim. Biophys. Acta. 985, 229–232.
295. “Determination of the structure of a membrane incorporated ion channel. Solid state NMR studies of gramicidin A.” Smith, R., Thomas, D.E., Separovic, F., Atkins, A.R. and Cornell, B.A. (1989) Biophys. J. 56, 307–314.
296. “A model for gramicidin A’–phospholipid interactions in bilayers.” Cornell, B.A. and Separovic, F. (1988) Eur. Biophys. J. 16, 299–306.
297. “Side chain and backbone conformation of gramicidin A in lipid bilayer membranes.” Cornell, B.A., Separovic, F. and Smith, R. (1988) in Transport through Membranes: Carriers, Channels and Pumps. A. Pullman, J. Jortner and B. Pullman (eds.), Kluwer Academic Publishers: Dordrecht, Neth. pp289–295.
298. “Excitation of triple quantum NMR coherences in solids by hard rf pulses.” Hutchison, W.D., Separovic, F., Cornell, B. and Bowden, G.J. (1988) Chem. Phys. Lett. 144, 87–89.
299. “MQ NMR hard and soft pulses for I=1 spin systems. Raman multiple quantum NMR.” Bowden, G.J., Hutchison, W.D. and Separovic, F. (1988) J. Magn. Reson. 79, 413–428.
300. “The effect of gramicidin A on phospholipid bilayers.” Cornell, B.A., Weir, L.E. and Separovic, F. (1988) Eur. Biophys. J. 16, 113-119.
301. “Conformation and orientation of gramicidin A in oriented phospholipid bilayers measured by solid state carbon–13 NMR.” Cornell, B.A., Separovic, F., Baldassi, A.J. and Smith, R. (1988) Biophys. J. 53, 67–76.
302. “Characterisation of dodecylphosphocholine–myelin basic protein complexes.” Mendz, G.L., Moore, W.J., Kaplin, I.J., Cornell, B.A., Separovic, F., Miller, D.J. and Brown, L.R. (1988) Biochemistry 27, 379–386.
303. “EPR and NMR measurements on high temperature superconductors.” Bowden, G.J., Elliston, P.R., Wan, K.T., Dou, S.X., Easterling, K.E., Bourdillon, A.J., Sorrell, C.C., Cornell, B.A., and Separovic, F. (1987) J. Phys. C. Lett. 20, L545-L552.
304. “The effect of bacteriorhodopsin on the dynamics of lipid bilayers: a study by solid state C–13 nuclear magnetic resonance.” Cornell, B.A., Morris, C.A. Braach–Maksvytis, V.L.B. and Separovic, F. (1987) in Retinal Proteins. Yu. A. Ovchinnikov (ed.) VNU Science Press: Utrecht, Neth. pp285–293.
305. “Small unilamellar phospholipid vesicles and the theories of membrane formation.” Cornell, B.A., Middlehurst, J. and Separovic, F. (1986) Faraday Discuss. Chem. Soc. 81, 163–178.
306. “Membrane thickness and acyl chain length.” Cornell, B.A. and Separovic, F. (1983) Biochim. Biophys. Acta. 733, 189–193.
307. “P–31 nuclear magnetic resonance studies of the association of basic proteins with multilayers of diacyl phosphatidylserine.” Smith, R., Cornell, B.A., Keniry, M.A. and Separovic, F. (1983) Biochim. Biophys. Acta. 732, 492–498.
308. “Biological membranes are rich in low frequency motion.” Cornell, B.A., Hiller, R.G., Raison, J., Separovic, F., Smith, R., Vary, J.C. and Morris, C. (1983) Biochim. Biophys. Acta. 732, 473–478.
309. “A study of the angular dependence of NMR relaxation times in macroscopically oriented lyotropic liquid lamellar phases.” Pope, J.M., Walker, L., Cornell, B.A. and Separovic, F. (1982) Mol. Cryst. Liq. Cryst. 89, 137–150.
310. “The lower limit to the size of small sonicated phospholipid vesicles.” Cornell, B.A., Fletcher, G.C., Middlehurst, J. and Separovic, F. (1982) Biochim. Biophys. Acta. 690, 15–19.
311. “Low frequency motion in membranes: the effect of cholesterol and proteins.” Cornell, B.A., Davenport, J.B. and Separovic, F. (1982) Biochim. Biophys. Acta. 689, 337–345.
312. “The temperature dependence of the size of phospholipid vesicles.” Cornell, B.A., Fletcher, G.C., Middlehurst, J. and Separovic, F. (1981) Biochim. Biophys. Acta. 642, 375–380.
313. “Small phospholipid vesicles cannot undergo a fluid–to–crystalline phase transition.” Cornell, B.A., Middlehurst, J. and Separovic, F. (1980) Chem. Phys. Lett. 73, 569–571.
314. “The molecular packing and stability within highly curved phospholipid bilayers.” Cornell, B.A., Middlehurst, J. and Separovic, F. (1980) Biochim. Biophys. Acta. 598, 405–410.

Collaborations Outside of University of Melbourne, Australia

• Professor Mibel Aguilar, Department of Biochemistry & Molecular Biology, Monash University, Melbourne VIC
• Professor Alan Mark, School of Chemistry & Molecular Biosciences, University of Queensland, Brisbane QLD
• Assoc. Professor Lisa Martin, School of Chemistry, Monash University, Melbourne VIC
• Dr Tash Polyzos, CSIRO Materials Science & Engineering, Melbourne VIC

Africa & Asia

• Professor Graham Jackson, Department of Chemistry, University of Cape Town, South Africa
• Professor Akira Naito, Faculty of Engineering, Yokohama National University, Japan
• Assoc. Prof. Sherif Mahmoud, Biophysics & Laser Science Unit, Research Institute of Ophthalmology, Egypt

Europe

• Professor Gregor Anderluh, Department of Biochemistry, University of Ljublanja, Slovenia
• Professor Anne Ulrich, Institute of Biological Interfaces & Institute of Organic Chemistry, Karlsruhe Institute of Technology, Germany
• Dr Ivana Vinkovic Vrcek, Institute for Medical Research & Occupational Health, Zagreb, Croatia
• Professor Bonnie Wallace, Dept. of Crystallography, Birkbeck College, University of London, UK
• Professor Anthony Watts, Department of Biochemistry, University of Oxford, UK

North & South America

• Professor Gerardo Fidelio, Department of Chemistry, Universidad Nacional de Córdoba, Argentina
• Professor Ka Yee Lee, Department of Chemistry, University of Chicago, USA
• Professor Terry Lybrand, Chemistry & Pharmacology, Vanderbilt University, USA
• Professor Isabelle Marcotte, Department of Chemistry, University of Quebec at Montreal, Canada
• Professor Stanley Opella, Department of Chemistry & Biochemistry, University of California San Diego, USA

Membrane protein structure and interactions

Membrane proteins represent a significant challenge in structural biology. While it is estimated that a third of the human genome encodes for membrane proteins, the structures of relatively few membrane proteins are currently known. It will be some time before membrane protein structure determination becomes routine, yet over 40% of the drugs on the market today rely on the activity of membrane proteins for their efficacy. This project seeks to develop and apply novel techniques and approaches to study the structure and interactions of membrane proteins in-situ. A range of techniques for studying membrane interactions, including solid-state NMR, are being used for the study of membrane peptides and proteins.

Biologically active peptides: the relationship between structure and activity

We have identified peptides from the skin glands of frogs and toads which are amongst the most powerful biologically active compounds in the animal kingdom. The aims of this project are to investigate the relationship between the structure and biologically activity of chosen groups of peptides such as antimicrobial peptides, which may be used as alternatives to conventional antibiotics. Solid-state NMR is being used to determine the insertion and structure of these membrane-active peptides in model membranes and in live bacteria, since these peptides act by lysing cell membranes.

Membrane interactions and neurotoxicity of amyloid Abeta peptides from Alzheimer’s disease

A consequence of the increase in human life span is that age-related neurodegenerative diseases such as Alzheimer’s disease (AD) are more prevalent. Currently there are limited therapeutic treatments and no cure for AD. AD is characterized by the abnormal accumulation of amyloid beta peptide (Abeta) into insoluble aggregates called plaques but increasing evidence indicates that the soluble form of Abeta is the toxic species and may be mediated by binding to phospholipids in cell membranes. We seek to determine if there is a link between Abeta neurotoxicity and membrane binding. Co-localization of Abeta in model and cell membranes is being studied by solid-state NMR and other biophysical techniques.

Membrane structure and lipid interactions of pore-forming toxins by NMR.

The structure of the pore-forming proteins, equinatoxin II and listeriolysin O, is being studied in model cell membranes using solid-state NMR spectroscopy. The relationship of molecular structure to bioactivity and the nature of the pore-forming mechanism of the toxin will be determined (Toxins by NMR). The results will aid in understanding how toxins lyse cells and could lead to the design of improved antibiotic peptides. These newly developed techniques used for the structural determination of these membrane-associated proteins will be suitable for studying other membrane proteins and receptors of pharmaceutical importance. Listen to Up Close interview Pore me another: Understanding how toxins target & overcome membranes.