2022
DOI: 10.1002/bio.4225
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Investigation on the interaction between myricetin and dihydromyricetin with trypsin, α‐chymotrypsin, lysozyme by spectroscopy and molecular docking methods

Abstract: The interaction between myricetin and dihydromyricetin with trypsin, α-chymotrypsin and lysozyme was investigated using multispectral and molecular docking methods. The results of fluorescence quenching revealed that myricetin and dihydromyricetin could quench the intrinsic fluorescence of three different proteinases through a static quenching procedure. The binding constant and number of binding sites at different temperatures were measured. The thermodynamic parameters obtained at different temperatures show… Show more

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Cited by 8 publications
(2 citation statements)
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References 43 publications
(41 reference statements)
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“…Studies indicate that naringin can diminish the binding stability of lovastatin with pepsin and α ‐chymotrypsin, thereby elevating the concentration of free lovastatin (Yang et al, 2020). Nitrendipine and nimodipine have been shown in studies to be significantly affected by vitamin C in terms of its binding constants with human serum albumin and lysozyme (Meng et al, 2022, 2023). However, there are no reports on the influence of vitamin C on the pharmacokinetic effect.…”
Section: Introductionmentioning
confidence: 99%
“…Studies indicate that naringin can diminish the binding stability of lovastatin with pepsin and α ‐chymotrypsin, thereby elevating the concentration of free lovastatin (Yang et al, 2020). Nitrendipine and nimodipine have been shown in studies to be significantly affected by vitamin C in terms of its binding constants with human serum albumin and lysozyme (Meng et al, 2022, 2023). However, there are no reports on the influence of vitamin C on the pharmacokinetic effect.…”
Section: Introductionmentioning
confidence: 99%
“…Pepsin, trypsin and α-chymotrypsin are all present in the digestive system, which can degrade or hydrolyze proteins. [10][11][12] Pepsin is mainly released by cells in the stomach to break down food into peptides. [13] It is an endopeptidase that can catalyze the hydrolytic cleavage of digestive bonds near hydrophobic or aromatic amino acid residues.…”
mentioning
confidence: 99%