Robert Latour, Ph.D.
McQueen-Quattlebaum Professor
of Bioengineering
of Bioengineering
B.S. Chemical Engineering, 1979 University of Virginia
M.S. Bioengineering, 1986 University of Pennsylvania
Ph.D. Bioengineering, 1989 University of Pennsylvania
M.S. Bioengineering, 1986 University of Pennsylvania
Ph.D. Bioengineering, 1989 University of Pennsylvania
Research Interests
Implant Biomaterials and Biomechanics
Computational-Chemistry Based Biomolecular Modeling
Thermodynamics of Protein-Surface and
Protein-Cell Interactions
Computational-Chemistry Based Biomolecular Modeling
Thermodynamics of Protein-Surface and
Email:
Office: 501-2 Rhodes Research Center
Phone: 864.656.5552
Office: 501-2 Rhodes Research Center
Phone: 864.656.5552
Honors, Awards, and Professional Activities
Current Research
Molecular Simulation of Peptide-and Protein-Surface Interactions
When a biomaterial is placed in the body, proteins (which are bioactive molecules) rapidly adsorb to the implant surface. Cells that then come in contact with the implanted biomaterial thus directly interact with the adsorbed protein layer rather than the actual surface of the implant. Accordingly, protein adsorption represents one of the most fundamental controlling factors of implant biocompatibility. Although the importance of protein adsorption is widely acknowledged, the actual molecular-level events involved, and how to control them, are still not well understood, and implant surface design is thus largely relegated to trial-and-error approaches. Molecular simulation provides a relatively new and extremely valuable theoretical tool to investigate these types of interactions with the potential to revolutionize biomaterials surface design. Existing methods, however, have been developed for much different applications and must be adapted to address the problem of protein adsorption to biomaterials surfaces. In response to this need, we are developing empirical force-field-based molecular simulation methods that will enable us to accurately simulate protein adsorption behavior as a function of surface chemistry. Once developed, these methods will provide an excellent resource to complement experimental studies to guide the design of biomaterials surfaces to directly control protein adsorption and subsequent biological response for improved patient care.
Experimental Characterization of Peptide-and Protein-Surface Interactions
Very little is currently understood regarding the specific molecular mechanisms that determine how proteins adsorb to biomaterial surfaces, and subsequently, how this influences cellular response and biocompatibility. We are therefore developing experimental methods using state-of-the-art techniques, including surface plasmon resonance (SPR) spectroscopy, variable wavelength spectroscopic ellipsometry, and circular dichroism (CD) spectropolarimetry, to elucidate the fundamental governing factors responsible for how peptides and proteins adsorb to materials surfaces as a function of surface chemistry and how the process of adsorption influences the bioactivity of the adsorbed proteins and subsequent cellular responses. These studies are planned synergistically with molecular simulation studies in order to generate the experimental data needed to guide and validate the developed molecular simulation methods, while also using the molecular simulation results to enhance our understanding of the molecular events underlying experimentally observed behavior.
Recent Publications
Wei, Y. and Latour R.A., Determination of adsorption free energy for peptide-surface interactions by SPR spectroscopy, Langmuir, 24: 6721-6729 (2008).
Fears K.P., Creager S.E., Latour R.A., Determination of the Surface pK of Carboxylic- and Amine-Terminated Alkanethiols Using Surface Plasmon Resonance Spectroscopy, Langmuir, 24: 837-843 (2008).
Wang F., Stuart S.J., Latour R.A., Calculation of adsorption free energy for solute-surface interactions using biased replica-exchange molecular dynamics, Biointerphases, 3(1) March: 9-18 (2008).
Sun Y., Dominy B.N., Latour R.A., Comparison of solvation-effect methods
for the simulation of peptide interactions with a hydrophobic surface, J.
Comput. Chem., 28: 1883-1892 (2007).
Li X.F., O'Brien C.P., Collier G., Vellore N.A., Wang F., Bruce D.A., Stuart S.J., Latour R.A., An improved replica-exchange sampling
method: Temperature intervals with global energy reassignment (TIGER), J.
Chem. Phys., 127: 1-10 (2007)
Latour R.A., Thermodynamic perspectives on the design of protein adsorption-resistant surfaces that include protein-surface interactions, J. Biomed. Mater. Res., 78A: 843-854 (2006).
Sun Y. and Latour R.A., Comparison of implicit solvent models for the simulation of protein-surface interactions, J. Computational Chemistry, 27: 1908-1922 (2006).
Sousa A., Sengonul M., Latour R.A., Kohn J., Libera M., Selective protein adsorption on a phase-separated solvent-cast biopolymer blend, Langmuir, 22: 6286-6292 (2006).
Raut V.P., Agashe M.A., Stuart S.J., and Latour R.A., Molecular dynamics
simulations of peptide-surface interactions, Langmuir, 21: 1629-1639
(2005).
Vernekar V.N., Latour R.A., Adsorption Thermodynamics Of A Mid-Chain Peptide Residue On Functionalized SAM Surfaces Using SPR, Materials Research Innovations, 9-2: 337-353 (2005).
Hylton D.M., Shalaby S.W., and Latour R.A., Direct correlation between
adsorption induced changes in protein structure and platelet adhesion, J.
Biomed. Mater. Res., 73A: 349-358 (2005).
Agashe M., Raut V., Stuart S.J., and Latour R.A., Molecular Simulation to
Characterize the Adsorption Behavior of a Fibrinogen Gamma-Chain Fragment, Langmuir, 21: 1103-1117 (2005).
