ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking
Hypertension and type 2 diabetes are the major metabolic syndromes, often managed using synthetic ACE and DPP-IV inhibitors that may cause adverse effects on health. This study investigated Bambara groundnut protein hydrolysates as a natural source of dual ACE- and DPP-IV-inhibitory peptides. Protei...
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2025-05-01
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| author | Jirakrit Saetang Thaiyawat Haewphet Krisana Nilsuwan Soottawat Benjakul |
| author_facet | Jirakrit Saetang Thaiyawat Haewphet Krisana Nilsuwan Soottawat Benjakul |
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| description | Hypertension and type 2 diabetes are the major metabolic syndromes, often managed using synthetic ACE and DPP-IV inhibitors that may cause adverse effects on health. This study investigated Bambara groundnut protein hydrolysates as a natural source of dual ACE- and DPP-IV-inhibitory peptides. Protein isolates were hydrolyzed using Flavourzyme, and the resulting peptides were fractionated using membranes with different molecular weight cut-offs. Those fractions were then analyzed for enzyme inhibition. Peptides were identified by LC-MS/MS and screened using PeptideRanker and BIOPEP-UWM, followed by molecular docking against ACE (PDB: 1O8A) and DPP-IV (PDB: 1NU6). The >10 kDa and 5–10 kDa fractions showed the highest ACE- and DPP-IV-inhibitory activities, respectively. Some peptides such as YKDGLYSPHW, LPVSTPGKF, and EPWWPK displayed strong binding affinities (ΔG: −10.2 to −11.3 kcal/mol for ACE, −8.6 to −9.1 kcal/mol for DPP-IV) and interacted with key catalytic residues, including His387 and Glu411 in ACE, and Ser630, Glu205, and Phe357 in DPP-IV. These findings highlight the potential of Bambara groundnut hydrolysates or peptides as a source of natural ACE and DPP-IV inhibitors. |
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| publishDate | 2025-05-01 |
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| spelling | doaj-art-8212d8317d6b4e6faf28b385f94d55802025-08-20T01:56:20ZengMDPI AGBiology2079-77372025-05-0114551110.3390/biology14050511ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular DockingJirakrit Saetang0Thaiyawat Haewphet1Krisana Nilsuwan2Soottawat Benjakul3International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai 90110, Songkhla, ThailandInternational Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai 90110, Songkhla, ThailandInternational Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai 90110, Songkhla, ThailandInternational Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai 90110, Songkhla, ThailandHypertension and type 2 diabetes are the major metabolic syndromes, often managed using synthetic ACE and DPP-IV inhibitors that may cause adverse effects on health. This study investigated Bambara groundnut protein hydrolysates as a natural source of dual ACE- and DPP-IV-inhibitory peptides. Protein isolates were hydrolyzed using Flavourzyme, and the resulting peptides were fractionated using membranes with different molecular weight cut-offs. Those fractions were then analyzed for enzyme inhibition. Peptides were identified by LC-MS/MS and screened using PeptideRanker and BIOPEP-UWM, followed by molecular docking against ACE (PDB: 1O8A) and DPP-IV (PDB: 1NU6). The >10 kDa and 5–10 kDa fractions showed the highest ACE- and DPP-IV-inhibitory activities, respectively. Some peptides such as YKDGLYSPHW, LPVSTPGKF, and EPWWPK displayed strong binding affinities (ΔG: −10.2 to −11.3 kcal/mol for ACE, −8.6 to −9.1 kcal/mol for DPP-IV) and interacted with key catalytic residues, including His387 and Glu411 in ACE, and Ser630, Glu205, and Phe357 in DPP-IV. These findings highlight the potential of Bambara groundnut hydrolysates or peptides as a source of natural ACE and DPP-IV inhibitors.https://www.mdpi.com/2079-7737/14/5/511hydrolysatesmetabolic syndromelegumes3D structures |
| spellingShingle | Jirakrit Saetang Thaiyawat Haewphet Krisana Nilsuwan Soottawat Benjakul ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking Biology hydrolysates metabolic syndrome legumes 3D structures |
| title | ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking |
| title_full | ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking |
| title_fullStr | ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking |
| title_full_unstemmed | ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking |
| title_short | ACE- and DPP-IV-Inhibitory Peptides from Bambara Groundnut Hydrolysate: Elucidation Using Computational Tools and Molecular Docking |
| title_sort | ace and dpp iv inhibitory peptides from bambara groundnut hydrolysate elucidation using computational tools and molecular docking |
| topic | hydrolysates metabolic syndrome legumes 3D structures |
| url | https://www.mdpi.com/2079-7737/14/5/511 |
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