Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins
Abstract
:1. Introduction
2. Materials and Methods
2.1. Chemicals
2.2. Peptide Stability Study
2.3. Kinetics Study of ACE Inhibition
2.4. Molecular Docking Studies
2.5. Statistical Analysis
3. Results and Discussion
3.1. Effect of the Catalytic Activity of Angiotensin Converting Enzyme on Bioactive Peptides
3.2. Inhibition Kinetics of Bioactive Peptides toward ACE
3.3. Molecular Docking Studies
4. Conclusions
Author Contributions
Funding
Conflicts of Interest
References
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Peptides | Peptide Concentration (µM) | ||||
---|---|---|---|---|---|
1 | YLLLK | 250.0 | 125.0 | 62.0 | 31.0 |
2 | WAFS | 2000 | 1000 | 500 | 62.0 |
3 | GVQEGAGHYALL | 250.0 | 125.0 | 62.0 | 31.0 |
Bioactive Peptides | ||||||
---|---|---|---|---|---|---|
Incubation Time (h) | YLLLK | WAFS | GVQEGAGHYALL | |||
Peaks | Cleavage (%) | Peaks | Cleavage (%) | Peaks | Cleavage (%) | |
0.5 | 2 | 92 ± 2.8 | 3 | 43 ± 2.0 | 6 | 46 ± 1.5 |
1 | 4 | 93 ± 1.9 | 3 | 42 ± 1.6 | 6 | 65 ± 2.6 |
2 | 3 | 94 ± 3.0 | 3 | 63 ± 3.0 | 6 | 86 ± 3.1 |
3 | 2 | 94 ± 2.7 | 3 | 68 ± 3.4 | 6 | 97 ± 3.4 |
Peptides | ACE-Inhibitory Capacity (%) | Classification | |
---|---|---|---|
Without Pre-Incubation | With Pre-Incubation | ||
YLLLK | 100 ± 2.99 | 80 ± 2.04 | Substrate type |
WAFS | 55 ± 1.81 | 56 ± 1.34 | Pro-drug inhibitor |
GVQEGAGHYALL | 70 ± 1.15 | 75 ± 2.11 | Pro-drug inhibitor |
Peptide Sequence | Peptide Concentration (µM) | Km (mM) | Vmax (nmol/min) | (mM) | (nml/min) | CE (/) | Kiu (mM) |
---|---|---|---|---|---|---|---|
YLLLK | 250 125 62.0 31.0 | 0.3257 0.6862 1.2430 1.7820 | 11.19 14.21 25.72 25.88 | 34.35 20.70 20.69 14.52 | 0.155 | ||
Control | 0.00 | 1.452 | 31.67 | 21.81 | |||
WAFS | 2000 1000 500 62.0 | 2.807 5.712 5.051 3.455 | 33.63 56.81 59.79 61.03 | 11.98 9.94 11.83 17.66 | 2 | ||
Control | 0.00 | 1.456 | 31.87 | 21.88 | |||
GVQEGAGHYALL | 250 125 62.0 31.0 | 1.890 1.973 2.483 2.856 | 32.83 37.77 47.69 54.68 | 17.37 19.14 19.20 19.14 | 3.18 | ||
Control | 0.00 | 1.493 | 32.39 | 21.69 |
YLLLK | WAFS | GVQEGAGHYALL | |
---|---|---|---|
ACE Inhibition (%) | 100 | 55 | 70 |
ACE Inhibition (IC50) | 47 | 202 | 239 |
Electrostatic interaction (kJ/mol) | −122.247 | −115.733 | −115.098 |
Hydrophobic interaction (kJ/mol) | −1.048 | −0.535 | −0.512 |
Van der Waals (kJ/mol) | −4.115 | −2.267 | −1.396 |
Docking Score | −8.224 | −7.611 | −7.600 |
H-bonds | 7 | 5 | 5 |
Total Interaction | 15 | 15 | 13 |
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Zarei, M.; Abidin, N.B.Z.; Auwal, S.M.; Chay, S.Y.; Abdul Haiyee, Z.; Md Sikin, A.; Saari, N. Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins. Biomolecules 2019, 9, 569. https://doi.org/10.3390/biom9100569
Zarei M, Abidin NBZ, Auwal SM, Chay SY, Abdul Haiyee Z, Md Sikin A, Saari N. Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins. Biomolecules. 2019; 9(10):569. https://doi.org/10.3390/biom9100569
Chicago/Turabian StyleZarei, Mohammad, Najib Bin Zainal Abidin, Shehu Muhammad Auwal, Shyan Yea Chay, Zaibunnisa Abdul Haiyee, Adi Md Sikin, and Nazamid Saari. 2019. "Angiotensin Converting Enzyme (ACE)-Peptide Interactions: Inhibition Kinetics, In Silico Molecular Docking and Stability Study of Three Novel Peptides Generated from Palm Kernel Cake Proteins" Biomolecules 9, no. 10: 569. https://doi.org/10.3390/biom9100569