Exploring the binding interaction between bovine serum albumin and perindopril as well as influence of metal ions using multi-spectroscopic, molecular docking and DFT calculation

Insights into the interaction between the kusaginin and bovine serum albumin: Multi‐spectroscopic techniques and computational approaches

“…A blue shift of the maximum emission wavelength (from 343 to 327 nm) was observed, which can be explained by the fact that the changes in the environment of the fluorophore residues occurred and an increase of hydrophobicity in the vicinity of this residue took place. 10 These results indicated that there was a strong interaction between kusaginin and BSA.…”

“…4,5 It has been known for many years that serum albumin is an abundant and highly soluble plasma protein in the circulatory system, which has diverse and important physiological functions, such as sustaining plasma colloid osmotic pressure and pH of blood, and as carriers transfer of endogenous or exogenous compounds including indispensable amino acids, fatty acids, and a large variety of drugs. [6][7][8][9][10] The BSA protein contains 583 amino acids with 17 disulfide bonds and one free cysteine residue, molecular mass of 66 500 Da composed of a primarily α-helical secondary structure in physiological conditions. 8 Besides, BSA molecular consists of three homologous domains (labeled I, II, III), and each part is comprised of two subdomains.…”

“…9 Moreover, the significant contributors to the intrinsic fluorescence of BSA are dominated by the Trp-134 and Trp-213, located in subdomains IA and IIA, respectively (shown in Figure 1B). 10 In the present study, the interaction of BSA with kusaginin has been studied using multi-spectroscopic methods and computational approaches. The mechanism of fluorescence quenching of BSA by kusaginin was analyzed by the Stern-Volmer equation, while the binding constants (K a ) and binding sites (n) were obtained from the double logarithm regression plot, and the transfer efficiency of energy and distance between the BSA and kusaginin were measured based on the Förster theory of non-radiation energy transfer.…”

Albumin as a prospective carrier of the nitrosyl iron complex with thiourea and thiosulfate ligands under aerobic conditions

“…Fluorescence studies of the interaction of complex 1 with BSA Fluorescence spectroscopy is widely used to monitor the binding of drugs to albumin. 54 The intrinsic fluorescence of the protein is quenched due to the Förster energy transfer mechanism from excited tryptophan to various BSA-bound compounds that absorb in the region of protein fluorescence. 55 The addition of 7.19 × 10 −6 M complex 1 to BSA leads to fluorescence quenching of about 50% of the total intensity of protein (Fig.…”

Spectroscopic Evaluation of Chalcone Derivatives and their Zinc Metal Complexes: A Combined Experimental and Computational Approach on the Binding of the Complexes with the Serum Albumin

“…In total, 6 molecules were prepared and evaluated spectroscopically, both in situ and theoretically. More speci cally, we used TD-DFT studies [26][27][28][29][30][31], to evaluate our chalcone derivatives in terms of structure and activity, molecular docking [32][33][34][35], to evaluate their interaction with human serum albumin (HSA) and spectroscopy to evaluate their binding interactions with bovine serum albumin (BSA). The biological activity of the chalcone derivatives, was compared with the biological activity of their counter Zn complexes.…”