In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate
- Author
- Mahta Mirzaei (UGent) , Saeed Mirdamadi, Maliheh Safavi and Mahnaz Hadizadeh
- Organization
- Abstract
- The structure-function relation of YR-10 (YGKPVAVPAR) was investigated by synthesizing four structural analogs of that including YHR-10 (YGKHVAVHAR), GA-8 (GKPVAVPA), GHA-8 (GKHVAVHA), and PAR-3 (PAR). GA-8 (GKPVAVPA) was synthesized on the basis of simulated enzymatic gastrointestinal digestion performed by bioinformatics tools (expasy-peptide cutter). This study explains the molecular mechanisms for the interaction of synthetic peptides with ACE. The IC50 values of each were 139.554 +/- 2.3, 61.91 +/- 1.2, 463.230 +/- 3.56, 135.135 +/- 2.1, 514.024 +/- 5.86 mu M, respectively. Results indicated that Pro replacement with His in YR-10 and GA-8 increased ACE inhibitory activity respectively, by 55.63% and 70.82%. Removal of Tyr and Arg from respectively N and C terminal positions of YR-10, following in silico simulated gastrointestinal digestion caused the 3.31 fold decrease in ACE inhibitory activity. YHR-10 showed the best docking poses, and GHA-8 exhibited interaction with Zn2+. Lineweaver-Burk plots of most active peptides suggest that they act as noncompetitive inhibitors against ACE.
- Keywords
- ACE inhibitory activity, Structure-function, Synthetic peptides, Saccharomyces cerevisiae, ANGIOTENSIN-CONVERTING ENZYME, PURIFICATION, MECHANISM
Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8766030
- MLA
- Mirzaei, Mahta, et al. “In Vitro and in Silico Studies of Novel Synthetic ACE-Inhibitory Peptides Derived from Saccharomyces Cerevisiae Protein Hydrolysate.” BIOORGANIC CHEMISTRY, vol. 87, 2019, pp. 647–54, doi:10.1016/j.bioorg.2019.03.057.
- APA
- Mirzaei, M., Mirdamadi, S., Safavi, M., & Hadizadeh, M. (2019). In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate. BIOORGANIC CHEMISTRY, 87, 647–654. https://doi.org/10.1016/j.bioorg.2019.03.057
- Chicago author-date
- Mirzaei, Mahta, Saeed Mirdamadi, Maliheh Safavi, and Mahnaz Hadizadeh. 2019. “In Vitro and in Silico Studies of Novel Synthetic ACE-Inhibitory Peptides Derived from Saccharomyces Cerevisiae Protein Hydrolysate.” BIOORGANIC CHEMISTRY 87: 647–54. https://doi.org/10.1016/j.bioorg.2019.03.057.
- Chicago author-date (all authors)
- Mirzaei, Mahta, Saeed Mirdamadi, Maliheh Safavi, and Mahnaz Hadizadeh. 2019. “In Vitro and in Silico Studies of Novel Synthetic ACE-Inhibitory Peptides Derived from Saccharomyces Cerevisiae Protein Hydrolysate.” BIOORGANIC CHEMISTRY 87: 647–654. doi:10.1016/j.bioorg.2019.03.057.
- Vancouver
- 1.Mirzaei M, Mirdamadi S, Safavi M, Hadizadeh M. In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate. BIOORGANIC CHEMISTRY. 2019;87:647–54.
- IEEE
- [1]M. Mirzaei, S. Mirdamadi, M. Safavi, and M. Hadizadeh, “In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate,” BIOORGANIC CHEMISTRY, vol. 87, pp. 647–654, 2019.
@article{8766030,
abstract = {{The structure-function relation of YR-10 (YGKPVAVPAR) was investigated by synthesizing four structural analogs of that including YHR-10 (YGKHVAVHAR), GA-8 (GKPVAVPA), GHA-8 (GKHVAVHA), and PAR-3 (PAR). GA-8 (GKPVAVPA) was synthesized on the basis of simulated enzymatic gastrointestinal digestion performed by bioinformatics tools (expasy-peptide cutter). This study explains the molecular mechanisms for the interaction of synthetic peptides with ACE. The IC50 values of each were 139.554 +/- 2.3, 61.91 +/- 1.2, 463.230 +/- 3.56, 135.135 +/- 2.1, 514.024 +/- 5.86 mu M, respectively. Results indicated that Pro replacement with His in YR-10 and GA-8 increased ACE inhibitory activity respectively, by 55.63% and 70.82%. Removal of Tyr and Arg from respectively N and C terminal positions of YR-10, following in silico simulated gastrointestinal digestion caused the 3.31 fold decrease in ACE inhibitory activity. YHR-10 showed the best docking poses, and GHA-8 exhibited interaction with Zn2+. Lineweaver-Burk plots of most active peptides suggest that they act as noncompetitive inhibitors against ACE.}},
author = {{Mirzaei, Mahta and Mirdamadi, Saeed and Safavi, Maliheh and Hadizadeh, Mahnaz}},
issn = {{0045-2068}},
journal = {{BIOORGANIC CHEMISTRY}},
keywords = {{ACE inhibitory activity,Structure-function,Synthetic peptides,Saccharomyces cerevisiae,ANGIOTENSIN-CONVERTING ENZYME,PURIFICATION,MECHANISM}},
language = {{eng}},
pages = {{647--654}},
title = {{In vitro and in silico studies of novel synthetic ACE-inhibitory peptides derived from Saccharomyces cerevisiae protein hydrolysate}},
url = {{http://doi.org/10.1016/j.bioorg.2019.03.057}},
volume = {{87}},
year = {{2019}},
}
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