Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study.

ABSTRACT: 9-Hydroxyphenanthrene (9-OHPhe), the representative hydroxyl metabolite of phenanthrene, has generated increasing concern as it is potentially hazardous to organisms. Herein, multispectroscopic and molecular docking techniques were applied to investigate the molecular interaction of human serum albumin (HSA) with 9-hydroxyphenanthrene (9-OHPhe) under simulated physiological conditions. Steady-state fluorescence and time-resolved fluorescence spectral analysis showed that 9-OHPhe quenched HSA fluorescence through a mixed static and dynamic process. HSA can bind with 9-OHPhe to form a 1:1 complex, with binding constants of 1.28 × 10⁵, 1.36 × 10⁵, and 1.26 × 10⁵ L·mol^-1 at 298.15, 303.15, and 308.15 K, respectively. The strong binding between HSA an

SUBMITTER: Zhang J 

PROVIDER: S-EPMC7364716 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature