Interaction Study between ESIPT Fluorescent Lipophile-Based Benzazoles and BSA.

ABSTRACT: In this study, the interactions of ESIPT fluorescent lipophile-based benzazoles with bovine serum albumin (BSA) were studied and their binding affinity was evaluated. In phosphate-buffered saline (PBS) solution these compounds produce absorption maxima in the UV region and a main fluorescence emission with a large Stokes shift in the blue-green regions due to a proton transfer process in the excited state. The interactions of the benzazoles with BSA were studied using UV-Vis absorption and steady-state fluorescence spectroscopy. The observed spectral quenching of BSA indicates that these compounds could bind to BSA through a strong binding affinity afforded by a static quenching mechanism (K_q~10¹² L·mol^-1·s^-1). The docking simulations indicate th

SUBMITTER: Kroetz T 

PROVIDER: S-EPMC8586955 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature