2022
DOI: 10.1016/j.ultsonch.2022.106074
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Structural characterization and angiotensin-converting enzyme (ACE) inhibitory mechanism of Stropharia rugosoannulata mushroom peptides prepared by ultrasound

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Cited by 21 publications
(16 citation statements)
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“…KIGSRSRFDVT is a non-competitive inhibitor that binds at an inactive ACE site to inhibit ACE activity [ 66 ]. It was shown that Stropharia rugosoannulata peptides can bind to zinc ions, critical amino acids, or amino acid residues in the ACE active pocket, which inhibits the action of ACE [ 67 ]. Hydrolysis of A. bisporus scraps yielded three novel ACE inhibitory peptides; LVYP, VYPW, and YPWT which exhibited an average ACE inhibitory activity of 80.68%, and the IC 50 value was 0.9 mg/mL.…”
Section: Angiotensin-converting Enzyme (Ace) Inhibitory Propertymentioning
confidence: 99%
“…KIGSRSRFDVT is a non-competitive inhibitor that binds at an inactive ACE site to inhibit ACE activity [ 66 ]. It was shown that Stropharia rugosoannulata peptides can bind to zinc ions, critical amino acids, or amino acid residues in the ACE active pocket, which inhibits the action of ACE [ 67 ]. Hydrolysis of A. bisporus scraps yielded three novel ACE inhibitory peptides; LVYP, VYPW, and YPWT which exhibited an average ACE inhibitory activity of 80.68%, and the IC 50 value was 0.9 mg/mL.…”
Section: Angiotensin-converting Enzyme (Ace) Inhibitory Propertymentioning
confidence: 99%
“…ACE has three active sites (S1, S2, S1 , ) and Zn(II) [ 58 ], which are considered important for its inhibition. Among them, Pocket S1 contains three amino acids (Ala354, Glu384, and Tyr523), S2 contains five amino acids (Gln281, His353, Lys511, His513, and Tyr520), and S1 , (Glu162) contains one amino acid; these were considered the main active residues for interaction [ 45 , 47 , 48 ].…”
Section: Resultsmentioning
confidence: 99%
“…SRR14469700). The bath ultrasound working equipment is the same as in the literature [37] , developed by the Institute of Food Physical Processing of Jiangsu University. After the base material of the S.rugosoannulata peptide was separated by ultrafiltration, the peptide base material with a molecular weight of less than 3000 Da was collected, freeze-dried at −80 ℃ for 48 h, and then collected for standby.…”
Section: Methodsmentioning
confidence: 99%
“…The identification methods for the S.rugosoannulata peptide sequences are the same as those in the literature [37] . After desalting, dissolution (0.1 % formic acid, 5 % acetonitrile), and centrifugation (13500 rpm, centrifugation at 4 °C for 20 min) of the base material sample, 8 uL sample solution was taken for analysis and identification of peptide sequences by liquid chromatography-tandem mass spectrometry (LC-MS/MS).…”
Section: Methodsmentioning
confidence: 99%