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Unusual Binding of a Potential Biomarker with Human Serum Albumin.

Chem Asian J. 2013 Feb 12;

Authors: De D, Kaur H, Datta A


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 (Sudlow's sites I 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 site I and dansyl-L-proline (DP) as a competitor for site II. Steady-state and time-resolved fluorescence measurements affirm that neither of Sudlow's 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.

PMID: 23404770 [PubMed - as supplied by publisher]