Professor Frances SeparovicDeputy Director of the Bio21 Institute, University of Melbourne
Join us for this free lunch-time IHMRI Seminar. Lunch will be provided.
To attend, please email IHMRI by Friday 15 March for catering purposes.
Antimicrobial peptides (AMPs) present an alternative to conventional antibiotics but details of their mechanism of action and the basis for differences in potency observed between different bacterial strains remain unclear. Structural information is crucial for defining the molecular mechanism by which these peptides recognise and interact with a particular lipid membrane.
NMR structural investigations of cationic AMPs from Australian tree frogs in a range of different lipid systems will be discussed. In addition to studies in model membranes, solid-state NMR investigations of the AMP, maculatin 1.1, in live bacteria give us detailed insight into how these peptides form pores within bacterial membranes.
About the speaker
Professor Separovic played a key role in the determination of the molecular structure of the antibiotic gramicidin A and the bee toxin melittin within phospholipid membranes. Using novel solid-state NMR methods Frances has been able to determine the structure and dynamics of membrane polypeptides for biomolecular engineering applications.
Professor Separovic has organised 40 major national and international conferences and published over 230 peer reviewed papers. Her contributions to biophysics and NMR have been recognised by awards including 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 and an ISMAR Fellow. In 2017 Frances was named an IUPAC Distinguished Woman of Chemistry/Chemical Engineering and inducted in the Victorian Honour Roll of Women in 2018.