AI Article Synopsis
- Sudlow Site I of human serum albumin (HSA) is a binding site for various ligands, including warfarin.
- The study uses computational analysis and isothermal titration calorimetry (ITC) to examine the binding characteristics of warfarin, revealing a binding constant of 5.8 x 10(5) M(-1).
- ITC results indicate that warfarin binding involves the uptake of protons, suggesting stabilization through an ion-pair interaction with a specific amino acid in HSA.
Article 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 x 10(5) 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-.
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| http://dx.doi.org/10.1562/2006-02-23-RA-811 | DOI Listing |
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