Abstract Title:

The inhibitory mechanism of chlorogenic acid and its acylated derivatives onα-amylase and α-glucosidase.

Abstract Source:

Food Chem. 2022 Mar 15 ;372:131334. Epub 2021 Oct 5. PMID: 34638063

Abstract Author(s):

Shan Wang, Yue Li, Dejian Huang, Shangwei Chen, Yongmei Xia, Song Zhu

Article Affiliation:

Shan Wang


Due to the poor lipophilicity of chlorogenic acid (CA), five CA derivatives (C2-CA, C4-CA, C6-CA, C8-CA, and C12-CA) with different lipophilicities were synthesized using acylation catalyzed by lipase in present study. The inhibitory activities and mechanisms of CA and its derivatives onα-amylase and α-glucosidase were then determined. Results showed that the inhibitory activities of CA derivatives on α-amylase and α-glucosidase were enhanced as lipophilicity increased, and the inhibitory activities of C12-CA were stronger than those of CA. ICvalues of C12-CA were 13.30 ± 0.26 μmol/mL for α-amylase and 3.42 ± 0.10 μmol/mL for α-glucosidase. C12-CA possessed the smallest Kand Kvalues, and its inhibitory actions onα-amylase and α-glucosidase were stronger than those of CA and the other derivatives. Effects of C12-CA on microenvironments of amino acid residues and secondary structures of α-amylase and α-glucosidase were greater than those of CA and the other derivatives.

Study Type : In Vitro Study

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