Office: ISA 4206
Lab: ISA 4045, 4049
Ph.D. Physics, 2009, Carnegie Mellon University
Our primary research interests are centered on unveiling fundamental mechanisms dictating important membrane-associated biological processes. We use a multitude of approaches to achieve our goal. Experimentally, we use high-resolution atomic force microscopy to interrogate structural and dynamical properties of biological composites. Theoretically, we collaborate closely with molecular dynamic simulators to decipher short time scale events that are responsible for meso- and macro-scale properties discerned from experimental measurements.
1. Characterization of membrane structural and mechanical properties is important for elucidating molecular mechanisms of many membrane active antimicrobial peptides (AMPs). We use solution atomic force microscopy, force spectroscopy, micropipette aspiration, and vesicle leakage to study the perturbation of model lipid membranes affected by natural and synthetic AMPs.
2. Lipid membranes are suggested as potential targets by toxic protein aggregates. Using solution atomic force microscopy and several complementary techniques, we have studied aggregates (i.e. oligomers and fibrils) formed by a synthetic polyglutamine peptide. We also determined their disruptive effect on model lipid membrane's physical properties.
3. The M2 protein of influenza A virus was proposed to play a major role in virus packaging, assembly, and budding. Using solution atomic force microscopy and fluorescence microscopy, we studied the transmembrane domain of the M2 protein (M2TM) interacting with planar lipid bilayers and free-standing giant unilamellar vesicles (GUVs). We found that M2TM preferentially partitions into the liquid-disordered phase, M2TM increases the miscibility transition temperature of phase coexisting GUVs, and M2TM can elicit an array of vesicle shapes mimicking virus budding.
4. Lipid rafts were proposed to play an important role in a plethora of membrane-associated events (e.g. protein signaling and trafficking). Much of lipid raft properties can be inferred from the phase behavior of multi-component model lipid membranes. Using solution atomic force microscopy and fluorescence microscopy, we have obtained micron- and nanometer-sized phase separation in ternary and quaternary lipid bilayers.
|14466||PHZ 4702||001||Appl of Physics to Bio/Med I|
Students must complere BOTH PHY 2053 and PHY 2054 or PHY 2048 and PHY 2049 with C (or better) grades before
|11489||PHY 7910||021||Directed Research|