Investigation on the Interaction between Ilaprazole and Bovine Serum Albumin without or with Different C-Ring Flavonoids from the Viewpoint of Food–Drug Interference

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.

Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

“…It has been reported that the polyphenols of average human dietary intake is about 1 g/day, with two-third being flavonoids (Scalbert and Williamson, 2000). Up to now, there are only few studies on the influence of flavonoids on drugs-plasma proteins interaction (Mohseni-Shahri et al, 2014;Shi et al, 2012;Zhang et al, 2011). To our knowledge, the influence of flavonoids on NDP binding plasma proteins has still not been investigated.…”

β-Carotene and astaxanthin with human and bovine serum albumins

“…The absorption, distribution, metabolism and excretion properties, as the stability and toxicity of antioxidants, can be significantly affected by binding to serum albumin. First, the antioxidant-serum albumin interaction plays a dominant role in the bioavailability of antioxidants because the bound fraction of antioxidants is a depot, whereas the free fraction of antioxidants is active (Zhang et al, 2011). Second, if an antioxidant is metabolized and excreted from the body too fast because of low protein binding, the antioxidant cannot exert any benefit.…”

Spectroscopic analysis on structure–affinity relationship in the interactions of different oleanane‐type triterpenoids with bovine serum albumin

“…BSA contains two tryptophan residues, Trp212 (located within a hydrophobic pocket of the protein) and Trp134 (located on the surface of the protein molecule), which show intrinsic fluorescence (22). Fluorescence spectroscopy is an appropriate method to determine the interaction between small molecules and bioma cromolecules (23)(24)(25). In this work, we systematically evaluated the binding affinities of BSA with three oleanane-type triterpenoids, i.e.…”