Structure-function relationships in (poly)phenol-enzyme binding: Direct inhibition of human salivary and pancreatic α-amylases.

Autor: Visvanathan R; Department of Nutrition, Dietetics and Food, Monash University, BASE Facility, 264 Ferntree Gully Road, Notting Hill, VIC 3168, Australia; Victorian Heart Institute, Monash University, Victorian Heart Hospital, 631 Blackburn Road, Clayton, VIC 3168, Australia., Houghton MJ; Department of Nutrition, Dietetics and Food, Monash University, BASE Facility, 264 Ferntree Gully Road, Notting Hill, VIC 3168, Australia; Victorian Heart Institute, Monash University, Victorian Heart Hospital, 631 Blackburn Road, Clayton, VIC 3168, Australia., Barber E; Department of Nutrition, Dietetics and Food, Monash University, BASE Facility, 264 Ferntree Gully Road, Notting Hill, VIC 3168, Australia; Victorian Heart Institute, Monash University, Victorian Heart Hospital, 631 Blackburn Road, Clayton, VIC 3168, Australia., Williamson G; Department of Nutrition, Dietetics and Food, Monash University, BASE Facility, 264 Ferntree Gully Road, Notting Hill, VIC 3168, Australia; Victorian Heart Institute, Monash University, Victorian Heart Hospital, 631 Blackburn Road, Clayton, VIC 3168, Australia. Electronic address: gary.williamson1@monash.edu.
Jazyk: angličtina
Zdroj: Food research international (Ottawa, Ont.) [Food Res Int] 2024 Jul; Vol. 188, pp. 114504. Date of Electronic Publication: 2024 May 11.
DOI: 10.1016/j.foodres.2024.114504
Abstrakt: (Poly)phenols inhibit α-amylase by directly binding to the enzyme and/or by forming starch-polyphenol complexes. Conventional methods using starch as the substrate measure inhibition from both mechanisms, whereas the use of shorter oligosaccharides as substrates exclusively measures the direct interaction of (poly)phenols with the enzyme. In this study, using a chromatography-based method and a short oligosaccharide as the substrate, we investigated the detailed structural prerequisites for the direct inhibition of human salivary and pancreatic α-amylases by over 50 (poly)phenols from the (poly)phenol groups: flavonols, flavones, flavanones, flavan-3-ols, polymethoxyflavones, isoflavones, anthocyanidins and phenolic acids. Despite being structurally very similar (97% sequence homology), human salivary and pancreatic α-amylases were inhibited to different extents by the tested (poly)phenols. The most potent human salivary α-amylase inhibitors were luteolin and pelargonidin, while the methoxylated anthocyanidins, peonidin and petunidin, significantly blocked pancreatic enzyme activity. B-ring methoxylation of anthocyanidins increased inhibition against both human α-amylases while hydroxyl groups at C3 and B3' acted antagonistically in human salivary inhibition. C4 carbonyl reduction, or the positive charge on the flavonoid structure, was the key structural feature for human pancreatic inhibition. B-ring glycosylation did not affect salivary enzyme inhibition, but increased pancreatic enzyme inhibition when compared to its corresponding aglycone. Overall, our findings indicate that the efficacy of interaction with human α-amylase is mainly influenced by the type and placement of functional groups rather than the number of hydroxyl groups and molecular weight.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 The Author(s). Published by Elsevier Ltd.. All rights reserved.)
Databáze: MEDLINE
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