Steady State and Time-resolved Fluorescence Investigation of the Specific Binding of Two Chlorin Derivatives with Human Serum Albumin

Patel, Sunita; Datta, Anindya

doi:10.1021/jp072544u

Cited by 91 publications

(78 citation statements)

References 28 publications

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“…[39] Warfarin as a Marker for Sudlow's Site I Warfarin absorbs at around 305 nm in neat aqueous solution (pH 7), with an emission maximum at 390 nm, which is close to the values reported earlier (see the Supporting Information, Figures S1 and S2). [1,41] The formation of its complex with HSA is marked by small spectroscopic shifts, as reported elsewhere. [41,42] The binding constant of warfarin to Sudlow's site I in HSA, as reported in the literature, ranges from 2 10 5 to 5 10 5 m…”

Section: Introductionsupporting

confidence: 70%

“…[1][2][3][4] HSA consists of a single polypeptide chain that is made up of 585 amino acids with three a-helical domains (I-III). This structure can be further classified into two subgroups, A and B (Scheme 1 a).…”

Section: Introductionmentioning

confidence: 99%

“…[23] Herein, we extend this work towards an experimental determination of the location of BP(OH) 2 in HSA by using a competitivebinding technique. [1,14] Warfarin is used as a marker for site I and dansyl-l-proline is used as a competitor for site II. These experimental results are supported by computational molecular-docking experiments.…”

Section: Introductionmentioning

confidence: 99%

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Unusual Binding of a Potential Biomarker with Human Serum Albumin

Kaur

Datta

2013

Chemistry An Asian Journal

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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.

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Section: Introductionsupporting

confidence: 70%

Section: Introductionmentioning

confidence: 99%

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Unusual Binding of a Potential Biomarker with Human Serum Albumin

Kaur

Datta

2013

Chemistry An Asian Journal

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“…13 On the other hand, the intrinsic fluorescence of the tryptophan (Trp) and tyrosine (Tyr) residues in albumin have also been used as probes in binding analyses. [14][15][16] HSA has only one Trp residue in the sub-domain IIA region, which has been considered to be the major drug-binding site of HSA. 17,18 Therefore, the fluorescence of the Trp in HSA (Trp-HSA) is a useful probe for the binding to this site.…”

Section: Introductionmentioning

confidence: 99%

Binding Properties of Hydrophobic Molecules to Human Serum Albumin Studied by Fluorescence Titration

et al. 2009

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Two fluorescence modes were combined to analyze the binding properties of terminally substituted alkanes (CnX, X = COOH, OH, CHO, NH2) to human serum albumin (HSA). A competitive binding assay using an 8-anilino-1-naphthalenesulfonate (ANS) fluorescence probe provides information on all the hydrophobic binding sites in HSA. A binding assay using the intrinsic fluorescence of the tryptophan residue in HSA (Trp-HSA) provides information on the specific binding site close to the tryptophan residue. There are three fluorescence-active ANS binding sites in HSA, which can be classified into two types by their affinity for ANS. CnCOOH bound to all three ANS binding sites including the Trp-HSA site, however, it did not quench the fluorescence of Trp-HSA. CnCHO bound only to the Trp-HSA site with quenching of the fluorescence of Trp-HSA. By comparing the binding affinities of HSA for CnOH and CnCHO, it was concluded that the CnOH binding site is different from the CnCHO binding site. CnNH2 did not bind to any of the three ANS binding sites in HSA.

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“…It is not hard to study the quenching of protein intrinsic fluorescence since it has a single tryptophan residue. 13,14 Nowadays, nanopariticles are widely used in various fields, such as electronics, optics, genomics and proteomics. Titanium dioxide (TiO2) nanoparticles (NPs), one of the most typical nanoparticles, have been used in the bioanalytical field because of their large surface area, 4,15,16 enhanced chemical reactivity and easy penetration into cells.…”

Section: Introductionmentioning

confidence: 99%