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Unusual Binding of a Potential Biomarker with Human Serum Albumin

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Field Value
 
Title Unusual Binding of a Potential Biomarker with Human Serum Albumin
 
Creator DE, D
KAUR, H
DATTA, A
 
Subject albumin
biaryls
competition experiments
fluorescence
interfaces
DOUBLE-PROTON-TRANSFER
SURFACTANT INTERACTIONS
MOLECULAR-DYNAMICS
AUTOMATED DOCKING
FLUORESCENCE
STATE
PROTEINS
BOVINE
SINGLE
SITES
 
Description This study investigates the specific binding of a potential biomarker, [2,2-bipyridyl]-3,3-diol (BP(OH)2), with human serum albumin (HSA). The binding of BP(OH)2 at the two primary drug-binding sites on HSA (Sudlows sitesI and II) is explored by a competitive-binding study and monitored by considering the green-light emission from its diketo tautomer. Warfarin is used as a marker for siteI and dansyl-L-proline (DP) as a competitor for siteII. Steady-state and time-resolved fluorescence measurements affirm that neither of Sudlows sites is the binding locus of BP(OH)2. To gain an idea regarding the probable binding site of BP(OH)2, we perform molecular-docking studies, which reveal a close proximity of the probe to Trp-214 in subdomain IIA of HSA. Confirmation of this contention is achieved by studying the quenching of the fluorescence of Trp-214 in the presence of BP(OH)2. Moreover, static quenching seems to be responsible for the depletion of the fluorescence of Trp-214, as manifested by the invariance of the intrinsic fluorescence lifetime of Trp-214, as a function of the concentration of BP(OH)2. Based on displacement and quenching studies, supported by molecular docking, we propose that BP(OH)2 binds in a cleft that separates subdomains IIIA and IIB, which is in close proximity to Trp-214.
 
Publisher WILEY-V C H VERLAG GMBH
 
Date 2014-10-16T14:50:53Z
2014-10-16T14:50:53Z
2013
 
Type Article
 
Identifier CHEMISTRY-AN ASIAN JOURNAL, 8(4)728-735
http://dx.doi.org/10.1002/asia.201201060
http://dspace.library.iitb.ac.in/jspui/handle/100/15829
 
Language en