Is There Consistency between the Binding Affinity and Inhibitory Potential of Natural Polyphenols as alpha-amylase Inhibitors?

摘要

The inhibitory potential of natural polyphenols for alpha-amylases has attracted great interests among researchers. The structure-affinity properties of natural polyphenols binding to alpha-amylase and the structure-activity relationship of dietary polyphenols inhibiting alpha-amylase were deeply investigated. There is a lack of consistency between the structure-affinity relationship and the structure-activity relationship of natural polyphenols as alpha-amylase inhibitors. Is it consistent between the binding affinity and inhibitory potential of natural polyphenols as with alpha-amylase inhibitors? It was found that the consistency between the binding affinity and inhibitory potential of natural polyphenols as with alpha-amylase inhibitors is not equivocal. For example, there is no consistency between the binding affinity and the inhibitory potential of quercetin and its glycosides as alpha-amylase inhibitors. However, catechins with higher alpha-amylase inhibitory potential exhibited higher affinity with alpha-amylase.