Erin Wilfong

Erin received her B.A. in chemistry from The Ohio State University in 2003 and is currently enrolled in the MD/PhD program.  Her research focuses on understanding the thermodynamics of protein-ligand interactions and structure-activity relationships using stromelysin-1 (MMP-3) as a model system. 

Despite recent advances in synthetic organic chemistry, computational chemistry and structural biology, the molecular basis of affinity in aqueous solution remains poorly understood.  Additivity is a frequently invoked concept in ligand binding.  In the late 1970's, Jencks noted that the energetic consequence of linking two conceptual fragments, A and B, into a single AB ligand had an indeterminate effect on the energetics of ligand binding.  Using matrix metalloproteinase-3 (stromelysin-1) as a model system, two series of linkage ligands were created to investigate the origin and nature of the Jencksian interaction energy.  Contrary to previous speculation that such energies are primarily entropic in origin, our data demonstrate that, at least for stromelysin-1, additivity is an enthalpic phenomenon.  Possible molecular origins of this behavior and their consequences for ligand design under investigation.

e-mail: http://fds.duke.edu/db/aas/Chemistry/completedir.html