The following seminar will be held on Tuesday 25 September, 1.00-2.00pm in C17, Pope Building:
The Quest to Understand, Predict, and Control Protein-Surface Interactions through
the Synergistic Development of Molecular Simulation and Experimental Methods
Robert A. Latour, Ph.D.
McQueen-Quattlebaum Professor of Bioengineering
Clemson, University, Clemson, SC, USA
Robert A. Latour is the McQueen-Quattlebaum Professor in the Department of Bioengineering at Clemson University, Clemson, SC, USA and is presently on a year’s sabbatical as a visiting professor at King’s College-Strand Campus, University of London. Prof. Latour is in the rather unique position of supervising both experimental and molecular simulation laboratories, both of which are focused on the development of methods to study protein-surface interactions at the molecular level. This approach inherently lends to a high level of synergism of their efforts towards the joint goal of understanding, predicting, and controlling the interactions of peptides and proteins with synthetic materials.
Understanding protein-surface interactions is extremely important for a broad range of biotechnologies including medical implant biocompatibility, biosensors, biomineralization, biodefense, and bioseparations. Experimental methods alone are very limited in terms of their ability to probe the atomic-level detail that is required to understand adsorbed protein structure, which largely governs bioactivity. In contrast, molecular simulation methods have the inherent potential to provide atomistic detail. However, simulation methods must first be validated for this type of application. This requires the careful development and application of synergistic experimental and simulation methods, with experimental data used to validate the simulation methods so that subsequent simulation results can be used to better understand experimentally observed behavior. To provide this capability, we have developed a suite of complementary experimental methods using surface plasmon resonance spectroscopy, circular dichroism spectropolarimetry, and amino-acid-specific labeling/mass spectrometry to probe adsorption free energy, changes in secondary and tertiary structure, and adsorbed protein orientation. By comparing experimental data to simulation results, we are working to evaluate, modify, and validate methods to provide the capability to accurately simulate protein adsorption behavior to a broad range of material surfaces. Once properly developed, these methods have great potential for use as a powerful tool for biomaterial system design.