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Study of the interaction between doxepin and human serum albumin by spectroscopic methods ☆

Paper ID Volume ID Publish Year Pages File Format Full-Text
28747 44089 2006 6 PDF Available
Title
Study of the interaction between doxepin and human serum albumin by spectroscopic methods ☆
Abstract

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.

Keywords
Human serum albumin; Doxepin hydrochloride; Fluorescence quenching; Fluorescence resonance energy transfer; Thermodynamic parameters
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Study of the interaction between doxepin and human serum albumin by spectroscopic methods ☆
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 179, Issues 1–2, 1 April 2006, Pages 161–166
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
Price after discount Only $4.95
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