fulltext.study @t Gmail

Binding of trazodone hydrochloride with human serum albumin: A spectroscopic study

Paper ID Volume ID Publish Year Pages File Format Full-Text
28908 44104 2007 6 PDF Available
Title
Binding of trazodone hydrochloride with human serum albumin: A spectroscopic study
Abstract

The binding of trazodone hydrochloride (TZH) to human serum albumin (HSA) was investigated by spectroscopic techniques. Various binding parameters have been evaluated. Negative enthalpy and positive entropy values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of TZH to HSA. The distance, r between donor (HSA) and acceptor (TZH) was found to be 2.16 nm based on the Förster's theory of non-radiation energy transfer. The circular dichroism data indicated that the α-helicity of HSA decreased upon interaction with TZH. The binding constant of HSA–TZH was found to decrease in presence of common ions and hence, shortened the stored time of drug in blood plasma.

Keywords
Human serum albumin; Trazodone hydrochloride; Fluorescence quenching; Fluorescence resonance energy transfer; Thermodynamic parameters
First Page Preview
Binding of trazodone hydrochloride with human serum albumin: A spectroscopic study
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us
Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 185, Issues 2–3, 25 January 2007, Pages 239–244
Authors
, , , ,
Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us