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" |