Competing Interactions in Molecular Recognition from MM-PBSA Calculation

Feb 21, 2012 | 03:00 PM


Dr. Parimal Kar, Max Planck Institute for Colloids and Interfaces, Potsdam

Free energy calculations have become part of the standard repertoire of computationalbiochemical research due to their widespread applicability, reaching from the predictionof binding affinities of small drug-candidate compounds to the evaluation of relative stabilitiesof large biomacromolecular structures. Probably the most well-known end-point, implicitsolvent free energy method is the Molecular Mechanics Poisson–Boltzmann SurfaceArea (MM-PBSA) approach. MM-PBSA allows analyzing individual energy contributionsby means of a free energy decomposition, which gives additional insights into the energeticsof the investigated system. We shall show its application to HIV-1/HIV-2 proteaseinhibitorand neuraminidase-inhibitor systems. Our calculations agree well withexperiment and provide a detailed understanding of the molecular forces governing bindingand drug resistance that might assist in the design of efficient inhibitors against targetprotein.

Time & Location

Feb 21, 2012 | 03:00 PM