ISSN print edition: 0366-6352
ISSN electronic edition: 1336-9075
Registr. No.: MK SR 9/7
Flavonoids inhibiting glycation of bovine serum albumin: affinity–activity relationship
Quan Liu, Ting-Ting Chen, and Hui Cao
School of Chemistry and Chemical Engineering, Nantong University, Nantong, 226007, China
Abstract: Protein glycation leads to the formation of advanced glycation end-products (AGEs), which contribute to the pathogenesis of diabetic complications. The structure-activity relationship of dietary flavonoids for inhibiting the glycation of bovine serum albumin (BSA) in vitro was subjected to a detailed investigation. The structure-activity relationship revealed that: 1) the hydroxylation on ring B of the flavones enhanced the inhibition and the hydroxyl groups at the C-5 and C-7 positions of flavones favoured the inhibition; 2) the optimal number of hydroxyl groups on ring B of the flavonols was one (at the C-3 position) and the methylation of flavonols weakened the inhibition; 3) the methoxylation at the C-6 position and methylation at C-4' position of genistein clearly enhanced the inhibition; 4) the hydroxyl groups at the C-5 and C-7 positions of flavanones were in favour of the inhibition; 5) the glycosylation of flavonoids significantly weakened the inhibition. Obvious linear affinity-activity relationships exist between the BSA-flavonoid interaction and flavonoids as BSA glycation inhibitors (R2 = 0.76585). The flavonoids with a higher affinity to BSA exhibited a stronger inhibition of the glycation of BSA.
Keywords: flavonoids – glycation – BSA – flavonoid-BSA interaction – structure-activity relationship
Full paper is available at www.springerlink.com.
Chemical Papers 69 (3) 409–415 (2015)
Sunday, September 19, 2021