A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

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.

Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

“…e changes in the conformation and the microenvironment of BSA are explored by relating the changes in the spectrum of BSA in absence and after addition of 5d ( Figure 7). e identified peaks (Figure 8(a) and 8(b)) were as follows: peak a (Rayleigh scattering peak; λ ex = λ em ) and peak b (2 nd order scattering peak; λ em = 2ex) [46]. e intensity of peak a increased with the increasing concentration of 5d.…”

“…Synchronous Fluorescence Studies. Synchronous fluorescence studies provide information regarding the microenvironmental changes in the amino acids responsible for fluorescence of protein [44][45][46][47]. ese studies measure the shift in the λ em, which might have occurred due to variations near the chromophores of a molecule.…”

Probing the binding interaction of zinc (II) Schiff bases with bovine serum albumin: A spectroscopic and molecular docking study

“…[ 2,6 ] In order to design the target action of drug and possible sensitizers, a probe is required. Such study of binding interaction of numerous fluorophores with the serum protein is significant towards the application of functional materials in drug delivery, nanomedicine development, chemical receptors, sensors, [ 7–10 ] and so forth. The microenvironment surrounding the molecule greatly influences and affects the chemical and biological properties of various reactions carried out in ex situ and in vivo media.…”

Development of an Albumin–Polymer Bioconjugate via Covalent Conjugation and Supramolecular Interactions

“…66 Polar hydrogens and partial charges were added, and nonpolar hydrogens were merged for BSA and polymers. 62 All the dockings were repeated for three times by applying an exhaustiveness score of 20. The poses from the three independent runs were pooled, and the most favorable binding pose was selected.…”