Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities
Chickpea (<i>Cicer arietinum</i> L.) peptides can inhibit dipeptidyl peptidase IV (DPP-IV), an important type 2 diabetes mellitus therapeutic target. The molecular interactions between the inhibitory peptides and the active site of DPP-IV have not been thoroughly examined, nor have their...
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MDPI AG
2023-08-01
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| Series: | Pharmaceuticals |
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| Online Access: | https://www.mdpi.com/1424-8247/16/8/1109 |
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| author | José Antonio Mora-Melgem Jesús Gilberto Arámburo-Gálvez Feliznando Isidro Cárdenas-Torres Jhonatan Gonzalez-Santamaria Giovanni Isaí Ramírez-Torres Aldo Alejandro Arvizu-Flores Oscar Gerardo Figueroa-Salcido Noé Ontiveros |
| author_facet | José Antonio Mora-Melgem Jesús Gilberto Arámburo-Gálvez Feliznando Isidro Cárdenas-Torres Jhonatan Gonzalez-Santamaria Giovanni Isaí Ramírez-Torres Aldo Alejandro Arvizu-Flores Oscar Gerardo Figueroa-Salcido Noé Ontiveros |
| author_sort | José Antonio Mora-Melgem |
| collection | DOAJ |
| description | Chickpea (<i>Cicer arietinum</i> L.) peptides can inhibit dipeptidyl peptidase IV (DPP-IV), an important type 2 diabetes mellitus therapeutic target. The molecular interactions between the inhibitory peptides and the active site of DPP-IV have not been thoroughly examined, nor have their pharmacokinetic properties. Therefore, the predictions of legumin- and provicilin-derived DPP-IV inhibitory peptides, their molecular interactions with the active site of DPP-IV, and their pharmacokinetic properties were carried out. Ninety-two unique DPP-IV inhibitory peptides were identified. Papain and trypsin were the enzymes with the highest A<sub>E</sub> (0.0927) and lowest B<sub>E</sub> (6.8625 × 10<sup>−7</sup>) values, respectively. Peptide binding energy values ranged from −5.2 to −7.9 kcal/mol. HIS-PHE was the most potent DPP-IV inhibitory peptide and interacts with residues of the active sites S1 (TYR662) and S2 (GLU205/ARG125 (hydrogen bonds: <3.0 Å)), S2 (GLU205/GLU206 (electrostatic interactions: <3.0 Å)), and S2′ pocket (PHE357 (hydrophobic interaction: 4.36 Å)). Most peptides showed optimal absorption (76.09%), bioavailability (89.13%), and were non-toxic (97.8%) stable for gastrointestinal digestion (73.9%). Some peptides (60.86%) could also inhibit ACE-I. Chickpea is a source of non-toxic and bioavailable DPP-IV-inhibitory peptides with dual bioactivity. Studies addressing the potential of chickpea peptides as therapeutic or adjunct agents for treating type 2 diabetes are warranted. |
| first_indexed | 2024-03-10T23:39:59Z |
| format | Article |
| id | doaj.art-d9c571fedfdb44c88a6d075a09364563 |
| institution | Directory Open Access Journal |
| issn | 1424-8247 |
| language | English |
| last_indexed | 2024-03-10T23:39:59Z |
| publishDate | 2023-08-01 |
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| series | Pharmaceuticals |
| spelling | doaj.art-d9c571fedfdb44c88a6d075a093645632023-11-19T02:34:04ZengMDPI AGPharmaceuticals1424-82472023-08-01168110910.3390/ph16081109Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-BioactivitiesJosé Antonio Mora-Melgem0Jesús Gilberto Arámburo-Gálvez1Feliznando Isidro Cárdenas-Torres2Jhonatan Gonzalez-Santamaria3Giovanni Isaí Ramírez-Torres4Aldo Alejandro Arvizu-Flores5Oscar Gerardo Figueroa-Salcido6Noé Ontiveros7Nutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoNutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoNutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoNutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoNutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoPostgraduate Program in Health Sciences, Faculty of Biological and Health Sciences, University of Sonora, Hermosillo 83000, MexicoNutrition Sciences Postgraduate Program, Faculty of Nutrition Sciences, Autonomous University of Sinaloa, Culiacan 80010, MexicoClinical and Research Laboratory (LACIUS, CN), Department of Chemical, Biological, and Agricultural Sciences (DCQBA), Faculty of Biological and Health Sciences, University of Sonora, Navojoa 85880, MexicoChickpea (<i>Cicer arietinum</i> L.) peptides can inhibit dipeptidyl peptidase IV (DPP-IV), an important type 2 diabetes mellitus therapeutic target. The molecular interactions between the inhibitory peptides and the active site of DPP-IV have not been thoroughly examined, nor have their pharmacokinetic properties. Therefore, the predictions of legumin- and provicilin-derived DPP-IV inhibitory peptides, their molecular interactions with the active site of DPP-IV, and their pharmacokinetic properties were carried out. Ninety-two unique DPP-IV inhibitory peptides were identified. Papain and trypsin were the enzymes with the highest A<sub>E</sub> (0.0927) and lowest B<sub>E</sub> (6.8625 × 10<sup>−7</sup>) values, respectively. Peptide binding energy values ranged from −5.2 to −7.9 kcal/mol. HIS-PHE was the most potent DPP-IV inhibitory peptide and interacts with residues of the active sites S1 (TYR662) and S2 (GLU205/ARG125 (hydrogen bonds: <3.0 Å)), S2 (GLU205/GLU206 (electrostatic interactions: <3.0 Å)), and S2′ pocket (PHE357 (hydrophobic interaction: 4.36 Å)). Most peptides showed optimal absorption (76.09%), bioavailability (89.13%), and were non-toxic (97.8%) stable for gastrointestinal digestion (73.9%). Some peptides (60.86%) could also inhibit ACE-I. Chickpea is a source of non-toxic and bioavailable DPP-IV-inhibitory peptides with dual bioactivity. Studies addressing the potential of chickpea peptides as therapeutic or adjunct agents for treating type 2 diabetes are warranted.https://www.mdpi.com/1424-8247/16/8/1109chickpeabioactive peptidesDPP-IV inhibitorsin silicomolecular dockingADMET |
| spellingShingle | José Antonio Mora-Melgem Jesús Gilberto Arámburo-Gálvez Feliznando Isidro Cárdenas-Torres Jhonatan Gonzalez-Santamaria Giovanni Isaí Ramírez-Torres Aldo Alejandro Arvizu-Flores Oscar Gerardo Figueroa-Salcido Noé Ontiveros Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities Pharmaceuticals chickpea bioactive peptides DPP-IV inhibitors in silico molecular docking ADMET |
| title | Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities |
| title_full | Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities |
| title_fullStr | Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities |
| title_full_unstemmed | Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities |
| title_short | Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (<i>Cicer arietinum</i> L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities |
| title_sort | dipeptidyl peptidase iv inhibitory peptides from chickpea proteins i cicer arietinum i l pharmacokinetics molecular interactions and multi bioactivities |
| topic | chickpea bioactive peptides DPP-IV inhibitors in silico molecular docking ADMET |
| url | https://www.mdpi.com/1424-8247/16/8/1109 |
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