Seminar by Prof. Mibel Aguilar, Department of Biochemistry & Molecular Biology, Monash University, Australia, on "Biomembrane Plasticity – what, how and why of membrane structure and function"

01 Apr 2019
Seminar room, room no. 350, Chemistry Department (second floor)
Talk title : "Biomembrane Plasticity – what, how and why of membrane structure and function"
About Speaker
Professor Mibel Aguilar is a Bioanalytical and Biophysical Chemist at Monash University whose research focuses on biomembrane nanotechnology, peptide biomaterials and peptidomimetic drug design. She completed her PhD in Chemistry at the University of Melbourne studying the metabolism and toxicity of paracetamol. She then completed a Post Doctoral position at St Vincent’s Institute for Medical Research working on developing physical models for protein analysis and purification. She then moved to Monash University where her group now focuses on peptide-based biomaterials and drug design and biomembrane nanotechnology and are developing novel compounds that allow us to exploit the potential of peptides as drugs and biomaterials. Her group is currently applying their technology to the development of new compounds for treatment of cardiovascular disease and also developing novel self-assembling systems for the production of new biomaterials and nanomaterials for tissue engineering. Our membrane nanotechnology projects involve the development of new biosensor methods for the analysis of membrane-mediated processes such as apoptosis, G protein-coupled receptor function and antimicrobial peptide function. Her group’s work has transformed our understanding of how biomembranes control cell-based systems and introduced a new approach to the design of proteolytically stable bioactive peptides and biomaterials. She has published 203 papers and 27 book chapters, and edited a volume of Methods in Molecular Biology on HPLC applications. She has also supervised several PhD and Honours students and has served as secretary and co-Chair of the Australian Peptide Association. She is currently a member of the Science Planning Group on Epigenetics for the Asia-Pacific Office of the International Council for Science and the Biophysical Society / Institute of Physics (BPS/IOP) Publication Advisory Board.
Abstract
Biomolecular-membrane interactions play a critical role in the regulation of many important biological processes such as protein trafficking, cellular signalling and ion channel formation. Peptide/protein-membrane interactions can also destabilise and damage the membrane which can lead to cell death. Characterisation of the molecular details of these binding-mediated membrane destabilisation processes is therefore central to understanding cellular events such as antimicrobial action, membrane-mediated amyloid aggregation, and apoptotic protein induced mitochondrial membrane permeabilization. Optical biosensors have provided a unique approach to characterising membrane interactions allowing quantitation of binding events and new insight into the kinetic mechanism of these interactions. We have developed dual polarisation interferometry (DPI) techniques to allow biophysical analysis of membrane structure changes [1-3]. The unique advantage of DPI is that it allows real-time measurement of bilayer structure changes during peptide binding and results demonstrate that the mechanisms of bilayer disturbance differ significantly between different classes of peptides and proteins. The combination of DPI with other biophysical techniques now opens the door to redefining molecular mechanism of biomolecular interactions in which the membrane bilayer is a key player.