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Monatshefte für Chemie - Chemical Monthly

, Volume 151, Issue 1, pp 135–139 | Cite as

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

  • Hasmik A. ShilajyanEmail author
  • Karine R. Grigoryan
Original Paper

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

Keywords

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

Notes

Acknowledgements

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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Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2020

Authors and Affiliations

  1. 1.Faculty of ChemistryYerevan State UniversityYerevanArmenia

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