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

   Akbay, Nuriye; Tok, Tugba Taskin; Seferoglu, Zeynel; Gokoglu, Elmas

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.

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Akbay, N., Tok, T. T., Seferoglu, Z. ve Gokoglu, E. (2018). Investigation of binding properties of two ethidium derivatives with serum albumins: spectral and computational approach. JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS, 36(12), 3114–3121. doi:10.1080/07391102.2017.1380536

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