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

• Published in: Food chemistry Vol. 135; no. 3; pp. 1083 - 1090
• Main Authors: Shi, Shuyun, Zhang, Yuping, Xiong, Xiang, Huang, Kelong, Chen, Xiaoqin, Peng, Mijun
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.12.2012; Elsevier
• Subjects: 2-Pyridinylmethylsulfinylbenzimidazoles - chemistry; Animals; Binding constant; Biological and medical sciences; Bovine serum albumin; catechin; Cattle; drugs; Flavonoid; fluorescence; Food industries; Food-Drug Interactions; foods; Fundamental and applied biological sciences. Psychology; hydrogen bonding; infrared spectroscopy; Interaction; luteolin; Milk and cheese industries. Ice creams; nutrient-drug interactions; Pantoprazole; Protein Binding; quercetin; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Spectrum Analysis - methods; stomach ulcers; taxifolin; Bovine serum albumin; Pantoprazole; Flavonoid; Interaction; Binding constant; Binding; Drug; Bovine; Interference; Serum albumin; Method; Globular protein; Polyphenol; Milk protein; Vertebrata; Mammalia; Artiodactyla; Whey protein; Ungulata; Food
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2012.05.049

► Affinities of pantoprazole to BSA with or without flavonoids were investigated. ► Flavonoids decreased binding affinities of pantoprazole with BSA. ► The order of the influence was (+)-catechin>quercetin>luteolin>taxifolin. ► Flavonoids could not change the quchenching mechanism of pantoprazole with BSA. 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.