<i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism
Inhibition of dipeptidyl peptidase-4 (DPP-4) is an effective way to control blood glucose in diabetic patients. <i>Tenebrio (T.) molitor</i> is an edible insect containing abundant protein. <i>T. molitor</i> protein-derived peptides can suppress the DPP-4 activity. However, t...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-11-01
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| Series: | Foods |
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| Online Access: | https://www.mdpi.com/2304-8158/11/22/3626 |
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| author | Jiao Tan Jing Yang Xinyi Zhou Ahmed Mahmoud Hamdy Xilu Zhang Huayi Suo Yu Zhang Ning Li Jiajia Song |
| author_facet | Jiao Tan Jing Yang Xinyi Zhou Ahmed Mahmoud Hamdy Xilu Zhang Huayi Suo Yu Zhang Ning Li Jiajia Song |
| author_sort | Jiao Tan |
| collection | DOAJ |
| description | Inhibition of dipeptidyl peptidase-4 (DPP-4) is an effective way to control blood glucose in diabetic patients. <i>Tenebrio (T.) molitor</i> is an edible insect containing abundant protein. <i>T. molitor</i> protein-derived peptides can suppress the DPP-4 activity. However, the amino acid sequence and binding mechanism of these DPP-4 inhibitory peptides remain unclear. This study used the flavourzyme for <i>T. molitor</i> protein hydrolysis, identified the released peptides with DPP-4 inhibitory effect, and investigated the binding interactions of these peptides with DPP-4. The results showed that flavourzyme efficiently hydrolyzed the <i>T. molitor</i> protein, as demonstrated by the high degree of hydrolysis, disappearance of protein bands in SDS-PAGE, and changes to protein structure. The 4-h flavourzyme hydrolysates showed a good inhibitory effect on DPP-4 (IC<sub>50</sub> value of 1.64 mg/mL). The fragment of 1000–3000 Da accounted for 10.39% of the total peptides, but showed the strongest inhibitory effect on DPP-4. The peptides LPDQWDWR and APPDGGFWEWGD were identified from this fraction, and their IC<sub>50</sub> values against DPP-4 were 0.15 and 1.03 mg/mL, respectively. Molecular docking showed that these two peptides interacted with the DPP-4 active site via hydrogen bonding, hydrophobic interactions, salt bridge formation, π-cation interactions, and π-π stacking. Our findings indicated that <i>T. molitor</i> protein-derived peptides could be used as natural DPP-4 inhibitors. |
| first_indexed | 2024-03-09T18:20:37Z |
| format | Article |
| id | doaj.art-71a3744486a5456ea78cc129a0bcaa91 |
| institution | Directory Open Access Journal |
| issn | 2304-8158 |
| language | English |
| last_indexed | 2024-03-09T18:20:37Z |
| publishDate | 2022-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Foods |
| spelling | doaj.art-71a3744486a5456ea78cc129a0bcaa912023-11-24T08:21:43ZengMDPI AGFoods2304-81582022-11-011122362610.3390/foods11223626<i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding MechanismJiao Tan0Jing Yang1Xinyi Zhou2Ahmed Mahmoud Hamdy3Xilu Zhang4Huayi Suo5Yu Zhang6Ning Li7Jiajia Song8College of Food Science, Southwest University, Chongqing 400715, ChinaChongqing Engineering Research Center for Processing & Storage of Distinct Agricultural Products, Chongqing Technology and Business University, Chongqing 400067, ChinaWesta College, Southwest University, Chongqing 400715, ChinaDairy Science Department, Faculty of Agriculture, Assiut University, Assiut 71526, EgyptCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaChongqing Engineering Research Center for Processing & Storage of Distinct Agricultural Products, Chongqing Technology and Business University, Chongqing 400067, ChinaCollege of Food Science, Southwest University, Chongqing 400715, ChinaInhibition of dipeptidyl peptidase-4 (DPP-4) is an effective way to control blood glucose in diabetic patients. <i>Tenebrio (T.) molitor</i> is an edible insect containing abundant protein. <i>T. molitor</i> protein-derived peptides can suppress the DPP-4 activity. However, the amino acid sequence and binding mechanism of these DPP-4 inhibitory peptides remain unclear. This study used the flavourzyme for <i>T. molitor</i> protein hydrolysis, identified the released peptides with DPP-4 inhibitory effect, and investigated the binding interactions of these peptides with DPP-4. The results showed that flavourzyme efficiently hydrolyzed the <i>T. molitor</i> protein, as demonstrated by the high degree of hydrolysis, disappearance of protein bands in SDS-PAGE, and changes to protein structure. The 4-h flavourzyme hydrolysates showed a good inhibitory effect on DPP-4 (IC<sub>50</sub> value of 1.64 mg/mL). The fragment of 1000–3000 Da accounted for 10.39% of the total peptides, but showed the strongest inhibitory effect on DPP-4. The peptides LPDQWDWR and APPDGGFWEWGD were identified from this fraction, and their IC<sub>50</sub> values against DPP-4 were 0.15 and 1.03 mg/mL, respectively. Molecular docking showed that these two peptides interacted with the DPP-4 active site via hydrogen bonding, hydrophobic interactions, salt bridge formation, π-cation interactions, and π-π stacking. Our findings indicated that <i>T. molitor</i> protein-derived peptides could be used as natural DPP-4 inhibitors.https://www.mdpi.com/2304-8158/11/22/3626edible insectsdipeptidyl peptidase-4peptides identificationmolecular dockingenzymatic hydrolysis |
| spellingShingle | Jiao Tan Jing Yang Xinyi Zhou Ahmed Mahmoud Hamdy Xilu Zhang Huayi Suo Yu Zhang Ning Li Jiajia Song <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism Foods edible insects dipeptidyl peptidase-4 peptides identification molecular docking enzymatic hydrolysis |
| title | <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism |
| title_full | <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism |
| title_fullStr | <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism |
| title_full_unstemmed | <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism |
| title_short | <i>Tenebrio molitor</i> Proteins-Derived DPP-4 Inhibitory Peptides: Preparation, Identification, and Molecular Binding Mechanism |
| title_sort | i tenebrio molitor i proteins derived dpp 4 inhibitory peptides preparation identification and molecular binding mechanism |
| topic | edible insects dipeptidyl peptidase-4 peptides identification molecular docking enzymatic hydrolysis |
| url | https://www.mdpi.com/2304-8158/11/22/3626 |
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