Prediction of ACE-I Inhibitory Peptides Derived from Chickpea (Cicer arietinum L.): In Silico Assessments Using Simulated Enzymatic Hydrolysis, Molecular Docking and ADMET Evaluation
Abstract
:1. Introduction
2. Materials and Methods
2.1. Protein Sequences
2.2. Analysis of ACE-I Inhibitory Peptides from Chickpea (Cicer arietinum L.) Proteins
2.3. In Silico Proteolysis Analysis and Virtual Screening of ACE-I Inhibitory Peptides
2.4. Molecular Docking of Predicted ACE-Inhibitory Peptides from Chickpea Proteins on the ACE-I Binding Site
2.5. ADMET Prediction Analysis
3. Results and Discussion
3.1. ACE-I Inhibitory Peptides Prediction from Chickpea Seed Legumin and Provicilin
3.2. Molecular Interaction of Chickpea (Cicer arietinum L.) ACE-I Inhibitory Peptides and ACE-I
3.3. ADMET Analyses Showed That CP Are Bioavailable and Non-Toxic
4. Conclusions
Supplementary Materials
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Protein | A | B | In Silico Hydrolysis | ||
---|---|---|---|---|---|
Proteases | AE | BE | |||
Legumin | 0.4335 | 0.0201 | Pepsin | 0.0101 | 0.00112 |
Trypsin | 0.0101 | 0.00018 | |||
Chymotrypsin | 0.0282 | 0.00168 | |||
Gastrointestinal digestion | 0.0343 | 0.00206 | |||
Papain | 0.0605 | 0.00302 | |||
Alcalase | 0.0323 | 0.00273 | |||
Provicilin | 0.3642 | 0.0110 | Pepsin | 0.0155 | 0.00011 |
Trypsin | 0.0132 | 0.00058 | |||
Chymotrypsin | 0.0221 | 0.00035 | |||
Gastrointestinal digestion | 0.0419 | 0.00024 | |||
Papain | 0.0442 | 0.00139 | |||
Alcalase | 0.0287 | 0.00067 |
Peptide/Ligand | BIOPEP ID | Binding Energy (Kcal/Mol) | Protein | Location | Released by | EC50 (µM/L) | PubChem/Satpdb ID |
---|---|---|---|---|---|---|---|
Lisinopril | −8.6 | 5362119 | |||||
VVF | 9044 | −9.2 | Legumin | [147–149] | Papain | 35.45 | 7014911 |
VAF | 8126 | −8.6 | Legumin | [434–436] | GID; Chymotrypsin (A) | 35.8 | satpdb14951 |
[406–408] [434–436] | Alcalase | ||||||
IW | 7544 | −8.5 | Legumin | [457,458] | Alcalase | 4.7 | 7019084 |
RY | 3380 | −8.4 | Legumin | [193,194] | Chymotrypsin (A); Alcalase | 10.5 | 7021456 |
RF | 3489 | −8.2 | Legumin | [134,135] | Chymotrypsin (A) | 93 | 150964 |
[354,355] | Chymotrypsin (A); Pepsin (pH 1.3);Alcalase | ||||||
IVR | 7502 | −8.0 | Provicilin | [2–4] | GID | 0.81 | 25217595 |
YL | 3350 | −7.9 | Legumin | [182–183] | Papain; GID | 122 | 87071 |
VF | 3384 | −7.8 | Legumin | [103,104] | Chymotrypsin (A); GID; Alcalase | 9.2 | 6993120 |
[148,149] [403,404] | Alcalase | ||||||
Provicilin | [122,123] | Papain; Alcalase | |||||
[58,59] | Alcalase | ||||||
SF | 7685 | −7.7 | Provicilin | [176,177] | Papain; Chymotrypsin (A), Pepsin (pH 1.3); GID | 130.2 | 7009597 |
Legumin | [10,11] | Papain; Chymotrypsin (A), Pepsin (pH 1.3); GID | |||||
[347,348] | Papain | ||||||
AF | 7583 | −7.5 | Provicilin | [407,408] | Papain | 190 | 6992394 |
Legumin | [435,436] | Papain | |||||
KF | 7692 | −7.4 | Legumin | [124,125] | Alcalase | 28.3 | 151410 |
CF | 7751 | −7.3 | Legumin | [12,13] | Papain; Chymotrypsin (A), Pepsin (pH 1.3); GID; Alcalase | 1.96 | 25051327 |
[19,20] | Papain | ||||||
PR | 3537 | −7.2 | Provicilin | [150,151] | Papain; Trypsin; GID | 4.1 | 151004 |
Legumin | [178,179] | GID | |||||
TF | 8185 | −7.1 | Provicilin | [110,111] | GID | 18 | 7010580 |
DR | 10091 | −7.0 | Provicilin | [203,204] | Trypsin; GID | 110.5 | 16122509 |
Legumin | [440,441] | GID | |||||
LR | 9213 | −6.8 | Provicilin | [148,149] | Trypsin | 158 | 152914 |
IL | 9079 | −6.5 | Provicilin | [139,140] | Papain; GID | 54.95 | 7019083 |
[449,450] | Alcalase | ||||||
Legumin | [382,383] | Alcalase | |||||
AR | 7742 | −6.4 | Legumin | [390,391] | GID; Trypsin; Papain | 95.5 | 446132 |
[320,321] | Papain | ||||||
DG | 7681 | −5.8 | Provicilin | [23,24] | Papain | 190.1410 | 151148 |
[49,50] | Papain | ||||||
[405,406] | Papain | ||||||
VK | 7558 | −5.7 | Legumin | [247,248] | Trypsin; GID | 13 | 168058 |
[245,246] | Alcalase |
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Arámburo-Gálvez, J.G.; Arvizu-Flores, A.A.; Cárdenas-Torres, F.I.; Cabrera-Chávez, F.; Ramírez-Torres, G.I.; Flores-Mendoza, L.K.; Gastelum-Acosta, P.E.; Figueroa-Salcido, O.G.; Ontiveros, N. Prediction of ACE-I Inhibitory Peptides Derived from Chickpea (Cicer arietinum L.): In Silico Assessments Using Simulated Enzymatic Hydrolysis, Molecular Docking and ADMET Evaluation. Foods 2022, 11, 1576. https://doi.org/10.3390/foods11111576
Arámburo-Gálvez JG, Arvizu-Flores AA, Cárdenas-Torres FI, Cabrera-Chávez F, Ramírez-Torres GI, Flores-Mendoza LK, Gastelum-Acosta PE, Figueroa-Salcido OG, Ontiveros N. Prediction of ACE-I Inhibitory Peptides Derived from Chickpea (Cicer arietinum L.): In Silico Assessments Using Simulated Enzymatic Hydrolysis, Molecular Docking and ADMET Evaluation. Foods. 2022; 11(11):1576. https://doi.org/10.3390/foods11111576
Chicago/Turabian StyleArámburo-Gálvez, Jesús Gilberto, Aldo Alejandro Arvizu-Flores, Feliznando Isidro Cárdenas-Torres, Francisco Cabrera-Chávez, Giovanni I. Ramírez-Torres, Lilian Karem Flores-Mendoza, Pedro Erick Gastelum-Acosta, Oscar Gerardo Figueroa-Salcido, and Noé Ontiveros. 2022. "Prediction of ACE-I Inhibitory Peptides Derived from Chickpea (Cicer arietinum L.): In Silico Assessments Using Simulated Enzymatic Hydrolysis, Molecular Docking and ADMET Evaluation" Foods 11, no. 11: 1576. https://doi.org/10.3390/foods11111576