2020
DOI: 10.1016/j.bioorg.2020.104029
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In vitro inhibitory effects of Chinese bayberry (Myrica rubra Sieb. et Zucc.) leaves proanthocyanidins on pancreatic α-amylase and their interaction

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Cited by 36 publications
(27 citation statements)
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“…Probably, the interaction between procyanidins and α-amylase promotes the formation of procyanidin/α-amylase complexes that reduce its activity [11,39]. A recent study performing docking calculations to evaluate the inhibitory effect of Chinese berry extracts rich in proanthocyanidins on α-amylase found that the extracts induced conformational changes and modified the microenvironment polarity of some residues on the enzyme's active site, which explain the inhibitory effects of these extracts [12]. The docking calculations found that trimers presented the most efficient binding to the active site of α-amylase [12].…”
Section: Inhibition Of α-Amylase By Carménère Pomace Polyphenol Extractsmentioning
confidence: 99%
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“…Probably, the interaction between procyanidins and α-amylase promotes the formation of procyanidin/α-amylase complexes that reduce its activity [11,39]. A recent study performing docking calculations to evaluate the inhibitory effect of Chinese berry extracts rich in proanthocyanidins on α-amylase found that the extracts induced conformational changes and modified the microenvironment polarity of some residues on the enzyme's active site, which explain the inhibitory effects of these extracts [12]. The docking calculations found that trimers presented the most efficient binding to the active site of α-amylase [12].…”
Section: Inhibition Of α-Amylase By Carménère Pomace Polyphenol Extractsmentioning
confidence: 99%
“…A recent study performing docking calculations to evaluate the inhibitory effect of Chinese berry extracts rich in proanthocyanidins on α-amylase found that the extracts induced conformational changes and modified the microenvironment polarity of some residues on the enzyme's active site, which explain the inhibitory effects of these extracts [12]. The docking calculations found that trimers presented the most efficient binding to the active site of α-amylase [12]. These authors argued that this interaction is more potent than monomers and dimers, as trimers possess more H-bonds, present a stronger hydrophobic effect, and possess more π-π bonds.…”
Section: Inhibition Of α-Amylase By Carménère Pomace Polyphenol Extractsmentioning
confidence: 99%
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