UV/Vis and fluorescence study on the interaction of Ni(II) complex of Schiff base of glycine and chiral auxiliary (S)-2-[N-(N′-benzylprolyl)amino]benzophenone with bovine serum albumin

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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.

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This work was supported by the Republic of Armenia MES SCS, in the frame of protection financing of Basic Laboratory of the Chair of Physical and Colloids Chemistry of Yerevan State University.

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Correspondence to Hasmik A. Shilajyan.

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Shilajyan, H.A., Grigoryan, K.R. UV/Vis and fluorescence study on the interaction of Ni(II) complex of Schiff base of glycine and chiral auxiliary (S)-2-[N-(N′-benzylprolyl)amino]benzophenone with bovine serum albumin. Monatsh Chem 151, 135–139 (2020).

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  • Absorption spectra
  • Fluorescence spectroscopy
  • Ni(II)-(S)-BPB-Gly
  • Protein
  • Resonance energy transfer