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Probing interaction of human serum albumin with the tautomers of 3,4′,7,8-tetrahydroxyflavone by spectroscopic and mass spectrometric approaches

Paper ID Volume ID Publish Year Pages File Format Full-Text
28054 44057 2012 8 PDF Available
Title
Probing interaction of human serum albumin with the tautomers of 3,4′,7,8-tetrahydroxyflavone by spectroscopic and mass spectrometric approaches
Abstract

3,4′,7,8-Tetrahydroxyflavone (3,4′,7,8-tetraHF) is a kind of plant flavonol, and possesses anti-inflammatory, anti-nociceptive and anti-platelet effects. For understanding its pharmacology, the binding mechanism of 3,4′,7,8-tetraHF to a model protein, human serum albumin (HSA), was probed by fluorescence and UV absorption and mass spectrometric approaches. The binding affinities of the drug with the native HSA and its isomer were about 1.64 ± 0.54 × 105 L mol−1 and 0.68 ± 0.53 × 105 L mol−1, respectively. The UV absorption results showed that the hydroxyl groups for both the keto and enol forms of 3,4′,7,8-tetraHF were dissociated and the drug bound with the protein in anion. The fluorescence emission intensities and anisotropy of 3,4′,7,8-tetraHF were dramatically enhanced after interacting with the protein. The binding site of the drug on HSA was located on the motional restricted hydrophobic pocket of subdomain IIA, namely site I, and the drug–protein complex was mainly stabilized by electrostatic and ionic forces.

► Structural features for the tautomers of 3,4′,7,8-tetraHF has been characterized. ► Complex of 3,4′,7,8-tetraHF and HSA has been determined by TOF-MS method. ► Spectroscopic property of drug after binding to various isomers of HSA was probed. ► The binding location of the drug on HSA was determined and validated. ► Binding mechanism of the drug and protein was explored with multiple approaches.

Keywords
Human serum albumin; Tautomers; Binding mode; Fluorescence; Mass spectroscopy
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Probing interaction of human serum albumin with the tautomers of 3,4′,7,8-tetrahydroxyflavone by spectroscopic and mass spectrometric approaches
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 243, 1 September 2012, Pages 65–72
Authors
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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