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Diversified spectral and molecular docking techniques for biophysical study of the interaction between bovine serum albumin and risedronate sodium salt, a bisphosphonate for the treatment of bone diseases

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Document pages: 13 pages

Abstract: At 289, 297 and 305, the binding interaction between bovine serum albumin (BSA) and sodium risedronate (RSN) was studied by FT-IR (Fourier transform infrared), UV VIS (UV VIS), fluorescence (emission and synchronization), CD (circular dichroism) spectroscopy and computational (molecular docking) techniques   K temperature at pH 7.40 of physiological buffer. The conformational and secondary structure changes of BSA were observed by CD spectrum and curve fitting program, and applied to Fourier self deconvolution in FT-IR spectrum. The formation of bsa-rsn complex was confirmed by UV-Vis spectrum. The static quenching type of BSA by RSN was verified from stern Volmer equation and modified stern Volmer equation. Binding constant of 105 wa obtained to be confirming that there exists a strong binding interaction between BSA and RSN. Synchronous fluorescence shows that the microenvironment of tryptophan was altered, not tyrosine of BSA; in addition to this, the distance between tryptophan of BSA and RSN was found out from Forster’s theory of nonradiation energy transfer. The interaction between BSA and RSN mainly occurred as a result of hydrogen bonds and van der Waals forces, the process is exothermic and spontaneous, and it was achieved through van ’t Hoff equation. This interaction was affected by the presence of biologically active Fe2+, Ni2+, Ca2+, Mg2+, and Cd2+ ions and was also studied. The subdomain IIIA of BSA involved with RSN interaction was authenticated from molecular docking analysis.

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