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Spectroscopic and molecular docking elucidation to binding characteristics of bovine serum albumin with bupropion an aminoketone-medication for nicotine addiction
Manjushree Makegowda (1) , Revanasiddappa Hosakere Doddarevanna (2,*)
(1) Department of Chemistry, University of Mysore, Manasagangothri, Mysuru 570 006, Karnataka, India
(2) Department of Chemistry, University of Mysore, Manasagangothri, Mysuru 570 006, Karnataka, India
(*) Corresponding Author
Received: 08 Mar 2019 | Revised: 29 Apr 2019 | Accepted: 04 May 2019 | Published: 30 Jun 2019 | Issue Date: June 2019
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.
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University Grants Commission of Basic Scientific Research section (UGC-BSR) for awarding the fellowship under meritorious students, the CATERS CSIR-CLRI, Chennai, India.
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DOI Link: https://doi.org/10.5155/eurjchem.10.2.146-155.1845
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