Double-Site Binding and Anti-/Pro-oxidation of Luteolin on Bovine Serum Albumin Mediated by Copper(II) Coordination
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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 x 10(5) L center dot mol(-1) for Lut to n = 2 and K-a = 7.1 x 10(5) L center dot 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(II) coordination increased the antioxidant activity of luteolin by 60% in the inhibition of carbonyl formation from the oxidation of amino groups in the side chain of BSA induced by the peroxyl radical ROO center dot; however, it counteracted the antioxidant effects of luteolin and played pro-oxidative roles in BSA aggregation induced by (OH)-O-center dot.
Original language | English |
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Journal | ACS Omega |
Volume | 7 |
Issue number | 23 |
Pages (from-to) | 19521–19534 |
Number of pages | 14 |
ISSN | 2470-1343 |
DOIs | |
Publication status | Published - 2022 |
- RADICAL SCAVENGING EFFICIENCY, MOLECULAR DOCKING, IN-VITRO, FLAVONOIDS, COMPLEX, SPECTROSCOPY, PARAMETERS, CHAIN, CU2+, ACID
Research areas
ID: 312695739