کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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28747 | 44089 | 2006 | 6 صفحه PDF | دانلود رایگان |

The binding of doxepin hydrochloride (DH) to human serum albumin (HSA) was investigated by fluorescence, UV–vis absorption and circular dichroism (CD) techniques under simulative physiological conditions. The binding parameters have been evaluated by fluorescence quenching method. Negative enthalpy (ΔH°) and positive entropy (ΔS°) values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of DH to HSA. The distance r between donor (HSA) and acceptor (DH) was obtained according to the Förster's theory of non-radiation energy transfer. Spectral results revealed that the binding of DH to HSA induced conformational changes in HSA. The effect of common ions on the binding constant of DH–HSA was also examined.
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 179, Issues 1–2, 1 April 2006, Pages 161–166