Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination.

ABSTRACT: The interactions of luteolin (Lut) with bovine serum albumin (BSA) mediated by Cu(II) were investigated by spectroscopic, calorimetric, and molecular dynamic (MD) methods. Fluorescence studies showed that the binding of Lut to BSA was significantly enhanced by Cu(II) coordination with the number of binding sites and binding constant increasing from n = 1 and K _a = 3.2 × 10⁵ L·mol^-1 for Lut to n = 2 and K _a = 7.1 × 10⁵ L·mol^-1 for a 1:1 Cu(II)-luteolin complex, in agreement with the results from isothermal titration calorimetry (ITC). Site-specific experiments with warfarin and ibuprofen and MD confirmed that two binding sites of BSA were sequentially occupied by two Cu(II)-luteolin complexes. Cu(I

SUBMITTER: Song MT 

PROVIDER: S-EPMC9202249 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature