Investigating the predominant factors which drive receptor-ligand binding for inhibitors selective for MMP-13

COMP 338

Noel A. Carrascal, noelcjr@hotmail.com and Robert C. Rizzo, rizzorc@gmail.com. Department of Applied Mathematics and Statistics, Stony Brook University, Math Tower Room 3-129, Stony Brook, NY 11794
Matrix metalloproteinases (MMPs) are a highly homologous family of enzymes implicated in a broad variety of disease including cancer. Despite the initial excitement offered by first generation anti-cancer MMP inhibitors, little or no clinical efficacy was observed in human trials. In hindsight, and at least in part, the disappointing results are now thought to be a consequence of the fact that first generation inhibitors were too broad spectrum. In this study, we are using computational methods to investigate what drives binding for a recently reported series of compounds highly selective for MMP-13. Molecular dynamics simulations, binding free energy calculations, and other analysis are being used to characterize the predominant factors which drive ligand association in this system. A comparison of the results obtained from continuum (GB-MD) versus explicit solvent (TIP3P-MD) dynamics simulations will be presented.
 

Poster Session
6:00 PM-8:00 PM, Tuesday, August 21, 2007 BCEC -- Ballroom Foyer, Poster

Sci-Mix
8:00 PM-10:00 PM, Monday, August 20, 2007 BCEC -- Exhibit Hall - B2, Sci-Mix

Division of Computers in Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007