A.A. Bhattacharya

TL;DR: Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation.

TL;DR: A crystallographic study of five HSA-fatty acid complexes formed using saturated medium-chain and long-chain fatty acids reveals key similarities and significant differences in the modes of binding, and serves to rationalise much of the biochemical data on fatty acid interactions with albumin.

TL;DR: In this paper, the crystal structures at 2.5 A-resolution of HSA-myristate complexed with the R-(+) and S-(-) enantiomers of warfarin, a widely used anticoagulant, were determined.

TL;DR: In this paper, high resolution crystal structures of human serum albumin (HSA) with two of the most widely used general anesthetics, propofol and halothane, were described.

TL;DR: This work presents the first high-resolution crystal structures of HSA complexed with two important unsaturated fatty acids, the monounsaturated oleic acid and the polyunsaturated arachidonic acid, observed to occupy the seven binding sites distributed across the protein that are also bound by medium and long-chain saturated fatty acids.