Abstract
The binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. The conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. The formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. The static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. The binding constant of order 105 was 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.
Highlights
E binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis, fluorescence, Circular Dichroism (CD) spectrometric, and computational techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. e conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. e formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. e static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. e binding constant of order 105 was 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. e 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. is interaction was affected by the presence of biologically active Fe2+, Ni2+, Ca2+, Mg2+, and Cd2+ ions and was studied. e subdomain IIIA of BSA involved with RSN interaction was authenticated from molecular docking analysis
There are two absorption peaks with the red shifts (3 nm): the stronger one at 220 nm corresponding to the backbone of the BSA structure, and weaker one at 280 nm corresponding to the π → π∗ transition for tyrosine (Tyr), tryptophan (Trp), and Phenylalanine (Phe) residues of BSA as they belong to aromatic amino acids [21]
Summary
Academic Editor: Jacopo Sgrignani e binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. e conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. e formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. e static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. e binding constant of order 105 was obtained to be confirming that there exists a strong binding interaction between BSA and RSN. Academic Editor: Jacopo Sgrignani e binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. In 2010 survey, about 22 million women and 5.5 million men in European Union, 8 million women and 1 million men in United states, and Asian people who are at the highest risk were suffered from this disease [3, 4] Another bone-related issue is Paget’s disease which affects one or more bones but not complete skeleton to cellular reshaping and disfigurement such as skull, femur, pelvis, and vertebrae [5]. Erefore, the rate of evident distribution and elimination of drugs can be found out with help of protein-drug interaction studies. erefore, this study finds applications in medicinal science for designing drugs and in pharmaceutical industries to improve the drug delivery process
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