Investigation of binding properties of two ethidium derivatives with serum albumins: spectral and computational approach. Issue 12 (10th September 2018)

• Record Type: Journal Article
• Authors: Akbay, Nuriye; Taskin Tok, Tugba; Seferoğlu, Zeynel; Gökoğlu, Elmas
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 36:Issue 12(2018)
• Page Start: 3114
• Page End: 3121
• Publication Date: 2018-09-10
• Subjects: fluorescence quenching -- Stern–Volmer -- ethidium bromide -- serum albumin -- molecular docking; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2017.1380536
• Languages: English
• ISSNs: 0739-1102

Abstract

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 (ΔH and ΔS 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.