Effect of the glycosylation of flavonoids on interaction with protein Journal Article


Authors: Cao, H.; Wu, D.; Wang, H.; Xu, M.
Article Title: Effect of the glycosylation of flavonoids on interaction with protein
Abstract: In this paper, two flavonoid aglycones (baicalein, quercetin) and their glycosides (baicalin, quercitrin) were studied for their ability to bind protein by quenching the protein intrinsic fluorescence. From the spectra obtained, the bimolecular quenching constants, the apparent static binding constants, and binding sites values were calculated. The glycosylation of flavonoids decreases the binding affinity with protein. For quercetin and quercitrin, the binding constants for BSA were 3.65 × 10<sup>7</sup> and 6.47 × 10<sup>3</sup> L mol<sup>-1</sup>, respectively. For baicalein and baicalin, the binding constants were 4.54 × 10<sup>8</sup> and 1.63 × 10<sup>6</sup> L mol<sup>-1</sup>, respectively. © 2009 Elsevier B.V.
Keywords: animal; metabolism; animals; fluorescence; spectrometry, fluorescence; protein binding; quercetin; chemistry; glycosylation; drug derivative; binding site; bsa; flavonoid; fluorescence quenching; interaction; aglycones; baicalein; baicalin; bimolecular quenching constant; binding affinities; binding constant; flavonoids; intrinsic fluorescence; binding energy; binding sites; body fluids; esterification; fatty acids; fluorescence spectroscopy; phenols; sugars; quenching; bovine serum albumin; flavanone derivative; quercitrin; cattle; chemical structure; spectrofluorometry; flavanones; molecular structure; serum albumin, bovine
Journal Title: Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy
Volume: 73
Issue: 5
ISSN: 1386-1425
Publisher: Elsevier Inc.  
Date Published: 2009-09-01
Start Page: 972
End Page: 975
Language: English
DOI: 10.1016/j.saa.2009.05.004
PUBMED: 19493695
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 5" - "Export Date: 30 November 2010" - "CODEN: SAMCA" - "Source: Scopus"
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  1. Ming Ming Xu
    34 Xu