Angiotensin I-converting enzyme (ACE) inhibitory peptides have been shown to have antihypertensive effects and have been utilized for physiologically functional foods and pharmaceuticals. The ACE inhibitory ability of...Angiotensin I-converting enzyme (ACE) inhibitory peptides have been shown to have antihypertensive effects and have been utilized for physiologically functional foods and pharmaceuticals. The ACE inhibitory ability of a hydrolysate is de- termined by its peptide composition. However, the peptide composition of a hydrolysate depends on proteolytic enzyme and the hydrolysis conditions. In this study, the effect of process conditions on the ACE inhibitory activity of rice dregs hydrolyzed with a trypsin was investigated systematically using response surface methodology. It was shown that the ACE inhibitory activity of rice dregs hydrolysates could be controlled by regulation of five process conditions. Hydrolysis conditions for optimal ACE inhibition were defined using the response surface model of fractional factorial design (FFD), steepest ascent design, and central composite design (CCD).展开更多
Short peptides based on the tripeptides, Leu-Arg-Pro and Leu-Lys-Pro, were synthesized by microwave assisted solid-phase synthesis method, in order to make a search for potential inhibitors for angiotensin I-convertin...Short peptides based on the tripeptides, Leu-Arg-Pro and Leu-Lys-Pro, were synthesized by microwave assisted solid-phase synthesis method, in order to make a search for potential inhibitors for angiotensin I-converting enzyme（ACE） with minimum side effects in the treatment of hypertension. One peptide with the sequence Leu-Arg-Pro-Phe-Phe shows the strongest inhibition towards ACE with an IC50 value of 0.26 μmol/L in vitro. The study of structure-activity relationship shows that the introduction of a bulky group into the N-terminal of this series of inhibitors may enlarge steric hindrance, resulting in the poor inhibitory activity towards ACE. The inhibitory activity decreased in turn when L-Pro, D-Pro or Ac6c was at the C-terminal respectively. The binding interaction between each of these inhibitors and testicular ACE（tACE） was performed by molecular docking. The results suggest that Leu-Arg-Pro-Phe-Phe mainly occupied the S1 subsite of tACE, and made contact with tACE via seven H-bonds. It appeared that the site on the peptide that bound with tACE was influenced by the configuration of the amino acid, L or D-form, at the C-terminal of the peptide.展开更多
Background:Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme(ACE)activity and the regulation of blood pressure.However,the tr...Background:Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme(ACE)activity and the regulation of blood pressure.However,the traditional experimental screening method for ACE inhibitory peptides is time consuming and costly,accompanied with the limitations as incomplete hydrolysis and peptides loss during purification process.Virtual methods with the aid of computer can break such bottle-neck of experimental work.In this study,an attempt was made to establish a library of di-and tri-peptides derived from proteins of Phascolosoma esculenta,a kind of seafood,through BIOPEP(http://www.uwm.edu.pl/biochemia/index.php/pl/biopep),and to screen highly active ACE inhibitory peptides by molecular docking with the help of LibDock module of Discovery Studio 3.5 software.Results:Two hundred and eighty four(284)di-and tri-peptides,derived from P.esculenta proteins after a virtual hydrolysis with pepsin,trypsin and a mixture of pepsin and trypsin,were predicted to possess ACE inhibitory activity,among which there are 99 ACE inhibitory peptides with estimated IC_(50) less than 50μM.Nine peptides were synthesized for the comparison between the estimated and the experimentally determined IC_(50).The results indicated that errors between the estimated and measured log(1/IC_(50))are all less than 1.0 unit.Conclusions:Virtual method for peptide library construction and ACE inhibitory peptides screening efficiently demonstrated that P.esculenta proteins are prospect resource for food-origin ACE inhibitory peptide.展开更多
The valorization of vegetable by-products is a promising strategy to combat climate change and achieve global carbon neutrality goals.This study aimed to exploit the high-value utilization of garlic by-products and to...The valorization of vegetable by-products is a promising strategy to combat climate change and achieve global carbon neutrality goals.This study aimed to exploit the high-value utilization of garlic by-products and to investigate the antihypertensive effects and potential mechanisms of the resulting angiotensin I-converting enzyme(ACE)inhibitory peptides.After protein extraction,enzymatic hydrolysis,and activity-directed fractionation,a potent and highly stable ACE inhibitory peptide(IC_(50):31.38μmol/L)was obtained,which was identified as VWAS and acted as a competitive inhibitor.VWAS stably bound to key residues in the ACE active center mainly through hydrogen bonding interactions and effectively lowered blood pressure in spontaneously hypertensive rats via alleviating renal and cardiac injuries,improving endothelial dysfunction,and regulating the renal renin-angiotensin system,antioxidant system,and anti-inflammatory system.These findings suggested that garlic protein-derived peptide(VWAS)was a desirable candidate for antihypertensive functional foods and provided guidance for the high-value utilization of garlic by-products.展开更多
文摘Angiotensin I-converting enzyme (ACE) inhibitory peptides have been shown to have antihypertensive effects and have been utilized for physiologically functional foods and pharmaceuticals. The ACE inhibitory ability of a hydrolysate is de- termined by its peptide composition. However, the peptide composition of a hydrolysate depends on proteolytic enzyme and the hydrolysis conditions. In this study, the effect of process conditions on the ACE inhibitory activity of rice dregs hydrolyzed with a trypsin was investigated systematically using response surface methodology. It was shown that the ACE inhibitory activity of rice dregs hydrolysates could be controlled by regulation of five process conditions. Hydrolysis conditions for optimal ACE inhibition were defined using the response surface model of fractional factorial design (FFD), steepest ascent design, and central composite design (CCD).
基金Supported by the National High Technology Research and Development Program of China(No.2006AA10Z331)
文摘Short peptides based on the tripeptides, Leu-Arg-Pro and Leu-Lys-Pro, were synthesized by microwave assisted solid-phase synthesis method, in order to make a search for potential inhibitors for angiotensin I-converting enzyme（ACE） with minimum side effects in the treatment of hypertension. One peptide with the sequence Leu-Arg-Pro-Phe-Phe shows the strongest inhibition towards ACE with an IC50 value of 0.26 μmol/L in vitro. The study of structure-activity relationship shows that the introduction of a bulky group into the N-terminal of this series of inhibitors may enlarge steric hindrance, resulting in the poor inhibitory activity towards ACE. The inhibitory activity decreased in turn when L-Pro, D-Pro or Ac6c was at the C-terminal respectively. The binding interaction between each of these inhibitors and testicular ACE（tACE） was performed by molecular docking. The results suggest that Leu-Arg-Pro-Phe-Phe mainly occupied the S1 subsite of tACE, and made contact with tACE via seven H-bonds. It appeared that the site on the peptide that bound with tACE was influenced by the configuration of the amino acid, L or D-form, at the C-terminal of the peptide.
基金supported by‘National Natural Science Foundation of China(No.31301413)’‘National Major Science and Technology Projects of China(No.2012ZX09304009)’the‘Fundamental Research Funds for the Central Universities’,People's Republic of China.
文摘Background:Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme(ACE)activity and the regulation of blood pressure.However,the traditional experimental screening method for ACE inhibitory peptides is time consuming and costly,accompanied with the limitations as incomplete hydrolysis and peptides loss during purification process.Virtual methods with the aid of computer can break such bottle-neck of experimental work.In this study,an attempt was made to establish a library of di-and tri-peptides derived from proteins of Phascolosoma esculenta,a kind of seafood,through BIOPEP(http://www.uwm.edu.pl/biochemia/index.php/pl/biopep),and to screen highly active ACE inhibitory peptides by molecular docking with the help of LibDock module of Discovery Studio 3.5 software.Results:Two hundred and eighty four(284)di-and tri-peptides,derived from P.esculenta proteins after a virtual hydrolysis with pepsin,trypsin and a mixture of pepsin and trypsin,were predicted to possess ACE inhibitory activity,among which there are 99 ACE inhibitory peptides with estimated IC_(50) less than 50μM.Nine peptides were synthesized for the comparison between the estimated and the experimentally determined IC_(50).The results indicated that errors between the estimated and measured log(1/IC_(50))are all less than 1.0 unit.Conclusions:Virtual method for peptide library construction and ACE inhibitory peptides screening efficiently demonstrated that P.esculenta proteins are prospect resource for food-origin ACE inhibitory peptide.
基金supported by the Special Fund for Leading Talent in Mount Tai Industry of Shandong Province(TSCY20200121).
文摘The valorization of vegetable by-products is a promising strategy to combat climate change and achieve global carbon neutrality goals.This study aimed to exploit the high-value utilization of garlic by-products and to investigate the antihypertensive effects and potential mechanisms of the resulting angiotensin I-converting enzyme(ACE)inhibitory peptides.After protein extraction,enzymatic hydrolysis,and activity-directed fractionation,a potent and highly stable ACE inhibitory peptide(IC_(50):31.38μmol/L)was obtained,which was identified as VWAS and acted as a competitive inhibitor.VWAS stably bound to key residues in the ACE active center mainly through hydrogen bonding interactions and effectively lowered blood pressure in spontaneously hypertensive rats via alleviating renal and cardiac injuries,improving endothelial dysfunction,and regulating the renal renin-angiotensin system,antioxidant system,and anti-inflammatory system.These findings suggested that garlic protein-derived peptide(VWAS)was a desirable candidate for antihypertensive functional foods and provided guidance for the high-value utilization of garlic by-products.
