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.

Competitive Displacement Restores the Hyperpolarized 15N NMR Signal in Blood Plasma

“…The inhibitor generally bears some structural similarity to the substrate. Competitive inhibition is often used to study the interaction of drugs with their target proteins. , Competitive displacement in combination with 1 H and 19 F NMR (including HP- labeled reporter ligands) has become a powerful drug screening technique. − …”

“…Competitive inhibition is often used to study the interaction of drugs with their target proteins. 32,33 Competitive displacement in combination with 1 H and 19 F NMR (including HP- 19 reporter ligands) has become a powerful drug screening technique. 33−36 The binding constant of unlabeled tris(2-pyridylmethyl)amine to human serum albumin (HSA) was measured by isothermal titration calorimetry (ITC) (Figure S3).…”