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Investigation of binding properties of dicationic styrylimidazo[1,2‐a]pyridinium dyes to human serum albumin by spectroscopic techniques
Author(s) -
Özdemir Ayşe,
Gökoğlu Elmas,
Yalçın Ergin,
Gökoğlu Esra,
Seferoğlu Zeynel,
Tekinay Turgay
Publication year - 2017
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3153
Subject(s) - human serum albumin , chemistry , circular dichroism , fluorescence , pyridinium , van der waals force , quenching (fluorescence) , hydrogen bond , titration , absorption (acoustics) , photochemistry , analytical chemistry (journal) , crystallography , molecule , chromatography , organic chemistry , materials science , physics , quantum mechanics , composite material
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 © 2016 John Wiley & Sons, Ltd.