H. Shilajyan, K. Grigoryan
Jan 1, 2020
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0
Influential Citations
7
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Journal
Monatshefte für Chemie - Chemical Monthly
Abstract
Binding interaction of Ni(II) complex of Schiff base of glycine and chiral auxiliary (S)-2-[N-(N′-benzylprolyl)amino]benzophenone (Ni(II)-(S)-BPB-Gly) with bovine serum albumin (BSA) at different temperatures (293, 298, and 308 K) has been studied using UV/Vis and fluorescence spectroscopy methods. A gradual decrease in the Stern–Volmer constant with the increase in temperature showed the static mechanism of BSA fluorescence quenching in the presence of Ni(II)-(S)-BPB-Gly initiated by the formation of ground-state complex. Analysis of the binding constants, number of binding sites, and thermodynamic parameters (∆H0, ∆S0, ∆G0) suggested that Ni(II)-(S)-BPB-Gly spontaneously and exothermically binds to BSA mainly driven by hydrogen bonding and van der Waals forces. The binding distances between Ni(II)-(S)-BPB-Gly and BSA in the temperature range 293–308 K determined using Forster’s resonance energy transfer theory (found to be 2.413, 2.445, and 2.459 nm) showed that the binding properties decrease with the temperature rising.Graphic abstract