Dipeptidyl Peptidase IV Inhibitory Peptides from Chickpea Proteins (Cicer arietinum L.): Pharmacokinetics, Molecular Interactions, and Multi-Bioactivities

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

Chickpea (Cicer arietinum 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 AE (0.0927) and lowest BE (6.8625 × 10−7) 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.

Original languageEnglish
Article number1109
JournalPharmaceuticals
Volume16
Issue number8
DOIs
StatePublished - Aug 2023

Bibliographical note

Publisher Copyright:
© 2023 by the authors.

Keywords

  • ADMET
  • DPP-IV inhibitors
  • bioactive peptides
  • chickpea
  • in silico
  • molecular docking

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