Abstract:

Macroporous resin was used to separate the crude extract of Kalimeris and four polyphenol-rich fractions (F1, F2,
F3, and F4) were obtained. F2 was further purified by Sephadex LH-20 column chromatography and 3,5-dicaffeoylquinic
acid and 3,4,5-tricaffeoylquinic acid were obtained. Using the protein glycosylation reaction models of bovine serum
albumin-methylglyoxal (BSA-MGO) and bovine serum albumin-glyoxal (BSA-GO), we analyzed the inhibitory activity of
each component on protein glycosylation. The results showed that the content of polyphenols was in the order of F2 > F1 >
F3 > F4, and all the four fractions had good inhibitory effects on protein glycosylation in both models. In BSA-GO reaction
model, the inhibitory capacity against protein glycosylation was in the order of 3,5-dicaffeoylquinic acid > F2 > F3 > F1 >
crude extract of Kalimeris > F4. In BSA-MGO reaction model, the inhibitory capacity against protein gly cosylation was in
the order of 3,5-dicaffeoylquinic acid > F2 > crude extract of Kalimeris > F1 > F4 > F3. These results are consistent with the
inhibitory effect of 3,5-dicaffeoylquinic acid separated from F2. The 3,5-dicaffeoylquinic acid as a phenolic compound from
Kalimeris had a potent inhibitory effect on protein glycosylation induced by MGO or GO.

Key words: Kalimeris, polyphenols, 3,5-dicaffeoylquinic acid, protein non-enzymatic glycosylation