Multiple binding modes of ibuprofen in human serum albumin identified by absolute binding free energy calculations.

ABSTRACT: Human serum albumin possesses multiple binding sites and transports a wide range of ligands that include the anti-inflammatory drug ibuprofen. A complete map of the binding sites of ibuprofen in albumin is difficult to obtain in traditional experiments, because of the structural adaptability of this protein in accommodating small ligands. In this work, we provide a set of predictions covering the geometry, affinity of binding and protonation state for the pharmaceutically most active form (S-isomer) of ibuprofen to albumin, by using absolute binding free energy calculations in combination with classical molecular dynamics (MD) simulations and molecular docking. The most favorable binding modes correctly reproduce several experimentally identified binding locations, which include the two Su

SUBMITTER: Evoli S 

PROVIDER: S-EPMC5130592 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature