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Investigation on the interaction between ilaprazole and bovine serum albumin without or with different C-ring flavonoids from the viewpoint of food-drug interference.

Authors
Type
Published Article
Journal
Journal of Agricultural and Food Chemistry
1520-5118
Publisher
American Chemical Society
Publication Date
Volume
59
Issue
15
Pages
8499–8506
Identifiers
DOI: 10.1021/jf201796x
PMID: 21732691
Source
Medline
License
Unknown

Abstract

The interaction between ilaprazole and bovine serum albumin (BSA) has been investigated in the absence and presence of four popular flavonoids with different C-ring structures, quercetin, luteolin, taxifolin, and (+)-catechin, by means of fluorescence spectroscopy. The results indicated that ilaprazole had a strong ability to quench the intrinsic fluorescence of BSA, and site marker competitive experiments indicated that the binding of ilaprazole to BSA primarily took place in subdomain IIA. The quenching process of ilaprazole with BSA was easily affected by flavonoids,; however, they did not change the quchenching mechanism of ilaprazole with BSA, whereas all of the fluorescence quenching was initiated by a static quenching procedure combining with nonradiative energy transfer. The presence of flavonoids decreased the quenching constants of ilaprazole with BSA from 2.2 to 23.7% and decreased the binding constants from 73.7 to 98.3%, which depended on the different flavonoids' structures. The decreased binding constants and unchangeable spatial distance of ilaprazole with BSA by the introduction of quercetin, luteolin, and taxifolin may result from the competition of flavonoids and ilaprazole binding to BSA, whereas in the presence of (+)-catichin, decreased binding constants and increased spatial distance possibly resulted from the formation of a ternary ilaprazole-BSA-(+)-catechin complex. All of these results may have relevant consequences in rationalizing the interferences of common food to gastric ulcer treatments.

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