albumin - publications

Predict more albumin - ligand interactions now!



The influence of flavonoids on the binding of pantoprazole to bovine serum albumin by spectroscopic methods: With the viewpoint of food/drug interference.


Food Chem. 2012 Dec 1;135(3):1083-90


Authors: Shi S, Zhang Y, Xiong X, Huang K, Chen X, Peng M


Abstract

The interaction of pantoprazole to bovine serum albumin (BSA) has been investigated with and without four popular 5,7,3',4'-hydroxy-substituted flavonoids, quercetin, luteolin, taxifolin and (+)-catechin. The presence of flavonoids decreased binding constants of pantoprazole with BSA from 39.7% to 93.8%, which depended on flavonoid structures. Analysis of infrared spectroscopy (IR) and circular dichroism (CD) showed the binding of pantoprazole to BSA caused apparent change in secondary structure of BSA. The calculated values of spatial-distance indicated the existence of quercetin, luteolin and taxifolin may compete with pantoprazole binding to BSA, while the existence of (+)-catechin possibly formed ternary pantoprazole-BSA-(+)-catechin complex. However, all the fluorescence quenching was initiated by static quenching procedure irrespective of the absence or presence of flavonoids, while van der Waals force and hydrogen bonds played major roles for pantoprazole-BSA association. All above results may have relevant consequence in rationalising the interferences of common food to gastric ulcer treatments.

PMID: 22953828 [PubMed - in process]