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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


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    <subfield code="p">JOURNAL OF BIOMOLECULAR STRUCTURE &amp; DYNAMICS</subfield>
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    <subfield code="a">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.</subfield>
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    <subfield code="u">Hacettepe Univ, Dept Chem, TR-06800 Ankara, Turkey</subfield>
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    <subfield code="u">Istanbul Medeniyet Univ, Dept Chem, TR-34700 Istanbul, Turkey</subfield>
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