Abstract
One of the highly soluble protein presents in circulatory system of bovine body is bovine serum albumin (BSA). Bupropion hydrochloride (BRN) served to treat prime smoking cessation and disorder due to depressive. BRN binding to BSA was studied by molecular docking and lots of spectroscopic (UV-vis, emission, synchronous, 3D fluorescence, CD and FT-IR) methods at pH = 7.40. Static quenching with strong binding was obtained for BSA-BRN system by forming complex. Secondary structures, conformations and microenvironments of BSA were altered after BRN interaction. Distance between BRN and BSA was also achieved. Biologically active metal ions (Cu2+, Ca2+, Mg2+, Fe2+ and Zn2+) were also influenced on the BSA-BRN complex. Bonds of hydrogen and Van der Waals were major binding forces to stabilize BSA-BRN complex at site I (IIA) of BSA. Hence, binding of BRN to transport protein (BSA) is of prominent importance and these findings could be helpful for BRN pharmacology and potential clinical research.
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.
