Characterization of solute binding at human serum albumin site II and its geometry using a biochromatographic approach

41Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

Abstract

Chiral recognition mechanism relationships for binding at site II on human serum albumin (HSA) were investigated using D, L dansyl amino acids. Sodium phosphate salt was used as a solute-HSA interaction modifier. A new model was developed using a biochromatographic approach to describe the variation in the transfer equilibrium constant with the salt concentration, i.e., the nature of the interactions. The solute binding was divided into two salt concentration ranges c. For the low c values, below 0.03 M, the nonstereoselective interactions constituted the preponderant contribution to the variation in the solute binding with the salt concentration. For the high c values, above 0.03 M, the solute binding was governed by the hydrophobic effect and the stereoselective interactions. The different contributions implied in the binding process provided an estimation of both the surface charge density (σ/F) and the surface area of the site II binding cavity accessible to solvent, which were found to be equal to around 10.10-7 mol/m2 and 2 nm2. As well, the excess of sodium ions excluded by the solute transfer from the surface area of the pocket were about -0.7 for dansyl norvaline and -0.8 for dansyl tryptophan.

Cite

CITATION STYLE

APA

Peyrin, E., Guillaume, Y. C., & Guinchard, C. (1999). Characterization of solute binding at human serum albumin site II and its geometry using a biochromatographic approach. Biophysical Journal, 77(3), 1206–1212. https://doi.org/10.1016/S0006-3495(99)76972-9

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free