Abstract
The mechanism of binding of bromopyrogallol red (BPR) with bovine serum albumin (BSA) was investigated by fluorescence, absorption, circular dichroism (CD) and lifetime measurements. The analysis of fluorescence data indicated the presence of both dynamic and static quenching mechanism in the binding. Various binding parameters have been evaluated. The CD spectral data revealed the decrease in α-helical content of BSA from 70.7% (in free BSA) to 53.89% (in bound form) thereby indicating the conformational change in BSA upon binding. The thermodynamic parameters have also been evaluated. The binding average distance, r between the donor (BSA) and acceptor (BPR) was determined based on the Förster's theory and it was found to be 3.84 nm. The association constant of BPR–BSA decreased in the presence of common ions.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
