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1 September 2006 Binding of Warfarin Influences the Acid-Base Equilibrium of H242 in Sudlow Site I of Human Serum Albumin
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Abstract

Sudlow Site I of human serum albumin (HSA) is located in subdomain IIA of the protein and serves as a binding cavity for a variety of ligands. In this study, the binding of warfarin (W) is examined using computational techniques and isothermal titration calorimetry (ITC). The structure of the docked warfarin anion (W) to Site I is similar to that revealed by X-ray crystallography, with a calculated binding constant of 5.8 × 105 M−1. ITC experiments (pH 7.13 and I = 0.1) carried out in three different buffers (MOPs, phosphate and Tris) reveal binding of W is accompanied by uptake of 0.30 ± 0.02 protons from the solvent. This measurement suggests that the binding of W is stabilized by an ion-pair interaction between protonated H242 and the phenoxide group of W.

Jennifer L. Perry, Michael R. Goldsmith, T. Richard Williams, Kyle P. Radack, Trine Christensen, Justin Gorham, Melissa A. Pasquinelli, Eric J. Toone, David N. Beratan, and John D. Simon "Binding of Warfarin Influences the Acid-Base Equilibrium of H242 in Sudlow Site I of Human Serum Albumin," Photochemistry and Photobiology 82(5), 1365-1369, (1 September 2006). https://doi.org/10.1562/2006-02-23-RA-811
Received: 23 February 2006; Accepted: 21 March 2006; Published: 1 September 2006
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