Kinetics and Molecular Docking Studies of the Inhibitions of Angiotensin Converting Enzyme and Renin Activities by Hemp Seed (Cannabis sativa L.) Peptides
Abstract
Four novel peptide sequences (WVYY, WYT, SVYT, and IPAGV) identified from an enzymatic digest of hemp seed proteins were used for enzyme inhibition kinetics and molecular docking studies. Results showed that WVYY (IC50 = 0.027 mM) was a more potent (p < 0.05) ACE-inhibitory peptide than WYT (IC50 = 0.574 mM). However, WYT (IC50 = 0.054 mM) and SVYT (IC50 = 0.063 mM) had similar renin-inhibitory activity, which was significantly better than that of IPAGV (IC50 = 0.093 mM). Kinetics studies showed that WVYY had a lower inhibition constant (Ki) of 0.06 mM and hence greater affinity for ACE when compared to the 1.83 mM obtained for WYT. SVYT had lowest Ki value of 0.89 mM against renin, when compared to the values obtained for WYT and IPAGV. Molecular docking results showed that the higher inhibitory activities of WVYY and SVYT were due to the greater degree of noncovalent bond-based interactions with the enzyme protein, especially formation of higher numbers of hydrogen bonds with active site residues.
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Fractionation of hemp hydrolysates did not improve activity, and isolated peptides responsible for antihypertensive activity had similar IC50 values (17 mg/L for WVYY and 269 mg/L for WYT).
“Interestingly, fractionation of hemp hydrolysates did not improve activity and isolated peptides responsible for antihypertensive activity had similar IC 50 values (17 mg/L for WVYY and 269 mg/L for WYT, Girgih et al. 2014b).”
From Comparing the Effectiveness of Three Different Biorefinery Processes at Recovering Bioactive Products from Hemp (Cannabis sativa L.) Byproduct (2020) · cites this paper as Girgih et al. 2014b
Cites
Fitzgerald, C., Mora-Soler, L., Gallagher, E., O’Connor, P., Prieto, J., Soler-Vila, A., & Hayes, M. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301361c · Cited by 177 · see citing works
Girgih, A. T., Udenigwe, C. C., Li, H., Adebiyi, A. P., & Aluko, R. E. (2011) · Journal of the American Oil Chemists' Society · doi:10.1007/s11746-011-1841-9 · Cited by 174 · see citing works
Self-citationRegazzo, D., Da Dalt, L., Lombardi, A., Andrighetto, C., Negro, A., & Gabai, G. (2010) · Dairy Science & Technology · doi:10.1051/dst/2010009 · Cited by 26 · see citing works
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Setti, L., Samaei, S. P., Maggiore, I., Nissen, L., Gianotti, A., & Babini, E. (2020) · Food and Bioprocess Technology · doi:10.1007/s11947-020-02550-6 · Cited by 20 · see citing works
- Authors
- Girgih, A. T., He, R., & Aluko, R. E.
- Affiliations
- University of Manitoba (CA)
- Nanjing University of Finance and Economics (CN)
- Corresponding author
- Aluko, Rotimi E.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2014-04-25
- Volume
- 62
- Issue
- 18
- Pages
- 4135-4144
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2016621387
- Cited by
- 97
- References
- 3
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 7 · 2023: 7 · 2022: 16 · 2021: 6 · 2020: 15 · 2019: 15 · 2018: 6 · 2017: 8 · 2016: 2 · 2015: 3 · 2014: 1
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Health Sciences › Medicine › Oncology › Peptidase Inhibition and Analysis
- Keywords
- Cannabis sativa, angiotensin-converting enzyme inhibition, renin inhibition, bioactive peptides, peptide identification, enzyme inhibition kinetics, molecular docking, hydrogen bonding, antihypertensive peptides, protein digestion
- MeSH terms
- Renin Inhibitors, Angiotensin-Converting Enzyme Inhibitors, Cannabis, Enzyme Inhibitors, Kinetics, Peptidyl-Dipeptidase A, Plant Extracts, Renin, Seeds, Molecular Docking Simulation
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