Investigation of binding properties of two ethidium derivatives with serum albumins: spectral and computational approach

AKBAY N., TAŞKIN TOK T., SEFEROĞLU Z., GÖKOĞLU E.

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, vol.36, no.12, pp.3114-3121, 2018 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 36 Issue: 12
  • Publication Date: 2018
  • Doi Number: 10.1080/07391102.2017.1380536
  • Journal Name: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.3114-3121
  • Keywords: fluorescence quenching, Stern-Volmer, ethidium bromide, serum albumin, molecular docking, BOVINE, SPECTROSCOPY, COMPLEXES, BROMIDE, DOCKING, ORANGE, BSA, RED, DNA
  • Gazi University Affiliated: Yes

Abstract

The interaction mechanisms of two ethidium derivatives, 3,8-dibenzoylamino-5-ethyl-6-phenylphenantridinium chloride (E2) and 3,8-diphenylacetylamino-5-ethyl-6-phenylphenantridinium chloride (E3) with serum albumins (BSA and HSA) have been investigated by a combined experimental and computational approach. Fluorescence quenching and UV-vis results revealed that the interaction of derivatives with albumins resulted in formation of ground-state complexes and the obtained Stern-Volmer quenching constants designate the presence of a static component in the quenching mechanisms. Thermodynamic parameters (H and S values) point out the ionic interactions play the major role in E2-BSA, E2-HSA and E3-HSA complexes. The van der Waals interactions are dominant forces in E3-BSA complex. Moreover, the obtained results in this study were supported with computational analyzes which have same tendency.