An Insight Into The Interaction of Risedronate Sodium With Human Serum Albumin By Absorption, FT-IR, Fluorescence, SEM, Voltammetry And Molecular Docking Studies
Journal Title: IOSR Journal of Applied Chemistry (IOSR-JAC) - Year 2018, Vol 11, Issue 2
Abstract
Interaction between human serum albumin (HSA) and risedronate sodium (RDT) was investigated by employing (emission and synchronous) fluorescence, ultraviolet–visible (UV-Vis) absorption, Fourier transform infrared (FT-IR) spectroscopic methods, voltammetry, scanning electron microscope (SEM) and molecular docking studies at physiological buffer conditions (pH 7.4). Stern–Volmer and Modified Stern–Volmer equations showed that static quenching, Van’t Hoff equation determined the interaction is spontaneous process and the binding is through hydrogen bonds and vander Waals forces. FT-IR reveals that the secondary structure of HSA was altered upon interaction with RDT. UV-Vis, SEM and voltammetric studies were given the information on complex formed between HSA and RDT. The conformation and microenvironment of HSA were changed after the interaction of RDT this was studied by synchronous fluorescence. The calculated binding constant is of the order of 105 suggesting that very sTABLE binding. The effects of Fe2+, Cu2+ and Zn2+ ions were also studied on the binding interaction between HSA and RDT that yields low binding constant values. The binding sites for RDT are present in site III (sub-domain IB) were achieved by ligand displacement and molecular docking studies. This study gives us information on transportation, distribution and toxicity effect of RDT when it enters into human blood serum and it has wide applications in pharmaceutical industry, life sciences and clinical medicine.
Authors and Affiliations
Manjushree M, Hosakere D Revanasiddappa
Keywords
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- EP ID EP413968
- DOI 10.9790/5736-1102014054.
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