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Data · dataset · 2015

Binding of a chromen-4-one Schiff’s base with bovine serum albumin: capping with β-cyclodextrin influences the binding

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This work deals with the synthesis of 6-methyl-3-[(4′-methylphenyl)imino]methyl-4H-chromen-4-one (MMPIMC), its binding to β-cyclodextrin, and the influence of the cyclodextrin complexation on the compound’s binding to bovine serum albumin (BSA).

Description

The 1:2 stoichiometry for the complexation of MMPIMC with β-cyclodextrin is determined with the binding constant of 1.90 × 10 4 M −2 . The structure of host–guest complex plays a role in protein binding of MMPIMC.

One- and two-dimensional NMR spectra are used to determine the mode of binding of the guest to β-cyclodextrin cavity and the structure of the inclusion complex is proposed. The binding of MMPIMC with BSA in the absence and the presence of β-cyclodextrin is studied. The binding strengths of MMPIMC–BSA (1.73 × 10 5 M −1 ) and β-cyclodextrin-complexed MMPIMC–BSA (9.0 × 10 4 M −1 ) show difference in magnitude.

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The Förster Resonance Energy Transfer efficiency and the proximity of the donor and acceptor molecules, are modulated by β-cyclodextrin. Molecular modeling is used to optimize the sites and mode of binding of MMPIMC with bovine serum albumin.

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Chemistry · Engineering · Physics

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Provenance · 1 source records, 13 field assertions
SourceKeyLast seenRaw
DataCite10.6084/m9.figshare.1263908.v111 d agoJSON v1
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concepts[field].local:field:physicsmapping · DataCitevocabulary-mapper@1.0.0keywords['Physics']
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