Domain-Specific Association of a Phenanthrene-Pyrene-Based Synthetic Fluorescent Probe with Bovine Serum Albumin: Spectroscopic and Molecular Docking Analysis.

ABSTRACT: In this report, the interaction between a phenanthrene-pyrene-based fluorescent probe (PPI) and bovine serum albumin (BSA), a transport protein, has been explored by steady-state emission spectroscopy, fluorescence anisotropy, far-ultraviolet circular dichroism (CD), time-resolved spectral measurements, and molecular docking simulation study. The blue shift along with emission enhancement indicates the interaction between PPI and BSA. The binding of the probe causes quenching of BSA fluorescence through both static and dynamic quenching mechanisms, revealing a 1:1 interaction, as delineated from Benesi-Hildebrand plot, with a binding constant of ∼10⁵ M^-1, which is in excellent agreement with the binding constant extracted from fluorescence anisotropy measurements. The

SUBMITTER: Sasmal M 

PROVIDER: S-EPMC6644396 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature