Related Experiment Video
Updated: Aug 19, 2026

A Rapid and Quantitative Fluorimetric Method for Protein-Targeting Small Molecule Drug Screening
Published on: October 16, 2015
The binding of flurbiprofen to plasma proteins
Abstract:
The binding of flurbiprofen to human serum albumin and normal plasma was measured using ultracentrifugation. Flurbiprofen was bound in excess of 99% in all cases. Over the concentration range normally associated with therapy the data could be adequately described by a one-site binding model. The association constant decreased with increasing protein concentration, being 3.04 X 10(6) M-1 at an albumin concentration, of 2 g/100 ml and 1.19 X 10(6) M-1 at a concentration of 4 g/100 ml. Flurbiprofen binding showed no dependence on pH over the range 7.0 to 8.0.
Related Concept Videos
Drug Distribution: Plasma Protein Binding
Protein-Drug Binding: Mechanism and Kinetics
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In contrast,...
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be bound by...
Factors Affecting Protein-Drug Binding: Drug Interactions
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Hepatic Drug Clearance: Effect of Protein Binding
For low-extraction-ratio drugs that are less than 80% protein-bound, minor changes in protein binding...

