Interaction Between Bovine Serum Albumin and <i>Trans</i>-Resveratrol: Multispectroscopic Approaches and Molecular Dynamics Simulation.

ABSTRACT: Recent studies have increasingly focused on molecular interactions between small molecules and proteins, especially binding mechanisms and thermodynamics, using multispectroscopic and molecular dynamics approaches. This study elucidated the molecular interaction mechanism between bovine serum albumin (BSA) and trans-resveratrol (Res) through an integrated approach combining multispectroscopic analyses and molecular dynamics simulations. The fluorescence quenching study revealed a static quenching mechanism between BSA and Res, which was further confirmed via ultraviolet-visible (UV-Vis) absorption spectroscopy. In particular, K_SV decreased from 5.01 × 10⁴ M^-1 at 298 K to 3.99 × 10⁴ M^-1 at 318 K. Furthermore, the calculated K

SUBMITTER: Li X 

PROVIDER: S-EPMC12294381 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature