Investigation of binding properties of dicationic styrylimidazo[1,2-a]pyridinium dyes to human serum albumin by spectroscopic techniques

详细信息    查看全文

• 作者：Ayşe &Ouml ; zdemir ; Elmas G&ouml ; koğlu ; EsraYılmaz ; Ergin Yalç ; ın ; Esra G&ouml ; koğlu ; Zeynel Seferoğlu and Turgay Tekinay
• 刊名：Luminescence
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：32
• 期：1
• 页码：86-92
• 全文大小：494K
• ISSN：1522-7243

文摘

The binding interaction between two dicationic styrylimidazo[1,2-a]pyridinium dyes and human serum albumin (HSA) was investigated at physiological conditions using fluorescence, UV–vis absorption, and circular dichroism (CD) spectroscopies. Analysis of the fluorescence titration data at different temperatures suggested that the fluorescence quenching mechanism of HSA by these dyes was static. The calculated thermodynamic parameters (ΔG°, ΔH° and ΔS°) indicated that hydrogen bonding and van der Waals forces played a major role in the formation of the dye–HSA complex. Binding distances (r) between dyes and HSA were calculated according to Förster's non-radiative energy transfer theory. Studies of conformational changes of HSA using CD measurements indicate that the α-helical content of the protein decreased upon binding of the dyes. Copyright