Identification of competitive inhibitors for bovine serum albumin from dynamic combinatorial libraries containing a bienzyme system

Abstract

Three dynamic combinatorial libraries (DCLs) have been generated by using esterification, combined with a protocol based on size-exclusion chromatography (SEC) and HRMS. Compared with sulfuric acid and water-soluble lipase, the immobilized lipase could be recycled successfully. A new inhibitor towards bovine serum albumin (BSA) was discovered by the SEC-HRMS protocol. The binding of the new binder with BSA was investigated at different temperatures by fluorescence. The association constants K were determined by Stern–Volmer equation. The thermodynamic parameters were calculated according to the Van^'t Hoff equation. On the basis of the thermodynamic results, it was considered that the new compound was bound to BSA mainly by hydrophobic interaction.