Binding interactions and FRET between bovine serum albumin and various phenothiazine-/anthracene-based dyes: a structure-property relationship.

ABSTRACT: The present study demonstrates binding interactions and Förster resonance energy transfer (FRET) between bovine serum albumin (BSA) and a series of structurally and electronically diverse phenothiazine (PTZ) and anthracene (ANT) dyes. Upon selective excitation of tryptophan (Trp) residues of BSA, radiationless energy transfer to a dye takes place, resulting in fluorescence quenching of the former. Fluorescence quenching mechanisms, FRET parameters, possible locations, and binding constants of dyes with the BSA have been examined to deduce a structure-property relationship. The mechanism of quenching is apparently static in nature. PTZ dyes with heteroatoms and a pentyl tail (C5-PTZ) attached to them were found to have a stronger binding affinity with BSA as compared to ANT dyes. Stronger b

SUBMITTER: Bhuin S 

PROVIDER: S-EPMC8693680 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature