John F. Zaroslinski

TL;DR: The in vitro binding of warfarin by human serum albumin was studied at various temperatures and at pH 7.4 by a frontal gel filtration technique and showed that, for the therapeutic concentration range, Warfarin was over 99% bound to albumin present in physiological concentration.

TL;DR: Frontal analysis gel filtration, which previously has been shown to provide superior reproducibility, critical temperature control and improved accuracy for two-site resolution, was used and postulated that the binding of salicylate involves both hydrophobic and ionic contributions.

TL;DR: A generic model for the prediction of drug association constants to HSA is reported, which uses a pharmacophoric similarity concept and partial least square analysis (PLS) to construct a quantitative structure-activity relationship.

TL;DR: Using warfarin as a test system, the application of BIACORE SPR biosensors are validated to reliably determine binding constants for drug/HSA interactions and it is shown that the % bound values determined by SPR correlate with thevalues determined by solution-based methods.

TL;DR: The qualitative and quantitative aspects of capillary electrophoretic methods used to study drug-protein interactions, viz.

TL;DR: In this paper, the pH dependence of warfarin binding to human serum albumin has been studied by circular dichroism, fluorescence, and equilibrium dialysis, showing that albumin complexes at low drug to protein ratios parallel the neutral to base transition, occurring in the protein over the pH range 6 to 9.