Biophysical analysis of coreceptor modulation of TCR-MHC interactions. One of our research interests is to study the molecular mechanisms of T cell recognition. We have particular interest in understanding the trimolecular interactions between membrane bound T cell receptor (TCR-CD3 complex) and its ligand, the peptide-MHC complex (pMHC), and co-receptor molecules. We are using different biophysical approaches which include surface plasmon resonance, isothermal titration calorimetry and atomic force spectroscopy to study the influence of co-stimulatory molecules on the kinetics and thermodynamics of TCR-pMHC binding. The goal is to use integrated molecular and biophysical approaches to study membrane TCR-MHC interactions and to understand how these interactions are modulated by co-receptors during T cell development and activation.
Energetics and kinetics of monoclonal antibody binding to soluble HIV Envelope proteins. An additional interest of our lab involves biophysical characterization of soluble, recombinant human HIV-1 Envelope proteins (gp120 and gp140). We have employed surface plasmon resonance, analytical sedimentation equilibrium analysis, isothermal titration calorimetry and atomic force spectroscopy to characterize the antigenicity and study the energetics, kinetics and single molecule force measurements of the binding of anti-gp120 and anti-gp41 antibodies to several recombinant HIV-1 Envelope proteins. These studies have relevance in immunogen design for generating anti-HIV vaccines.
Education and Training
- Ph.D., University of Glasgow (Scotland), 1992