Open AccessMolecular Docking and Extended Spectroscopy to Binding Characterizations: Etoposide a Glycoside of Podophyllotoxin with Bovine Serum Albumin
Publication year - 2021
Publication title -
biointerface research in applied chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.216
H-Index - 11
ISSN - 2069-5837
DOI - 10.33263/briac121.264278
Subject(s) - bovine serum albumin , chemistry , hydrogen bond , etoposide , van der waals force , förster resonance energy transfer , spectroscopy , binding site , fluorescence , conformational change , biophysics , crystallography , biochemistry , molecule , organic chemistry , biology , physics , chemotherapy , quantum mechanics , genetics
A significant soluble protein, specifically bovine serum albumin (BSA) plays an efficient role in drug delivery, and etoposide (ETS) is used to cure various cancers. Binding interaction between ETS and BSA examined by 3D, emission, synchronous fluorescence’s, UV–vis, FT–IR, and CD spectroscopy’s in the association of computational at pH 7.40 with 293, 301 and 309 K. Formed complex between ETS and BSA dominates van der Waals and bonding of hydrogen’s at sub-domain IIIA. Strong binding of ETS-BSA leads to altering BSA’s structural and conformations statically. Energy transfer reveals ETS-BSA distance. Apart from this, ETS-BSA binding is affected by Mg2+, Cu2+, Fe2+, Ca2+, and Co2+ ions. This study may help in the drug development and discovery process.