Preparation and identification of novel DPP-IV inhibitory peptides from Musculus senhousei: Peptidomic analysis, molecular simulation, and validation
Bioactive peptides have been considered effective alternatives for the treatment of type 2 diabetes targeting the dipeptidyl peptidase-IV (DPP-IV). In this study, novel DPP-IV inhibitory peptides were prepared and identified from Musculus senhousei through two-stage chromatographic purification, pep...
| Autores: | , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/382117 |
| Acceso en línea: | http://hdl.handle.net/10261/382117 https://api.elsevier.com/content/abstract/scopus_id/85187363042 |
| Access Level: | acceso abierto |
| Palabra clave: | Asian date mussel Bioactive peptides LC-MS/MS Peptide-enzyme interaction bioactive compounds peptides |
| Sumario: | Bioactive peptides have been considered effective alternatives for the treatment of type 2 diabetes targeting the dipeptidyl peptidase-IV (DPP-IV). In this study, novel DPP-IV inhibitory peptides were prepared and identified from Musculus senhousei through two-stage chromatographic purification, peptidomic analysis, in silico screening, and validation. Furthermore, molecular simulation was employed to analyze the interaction from a molecular perspective. Results showed that Musculus senhousei hydrolysate produced by 8 h Neutrase hydrolysis exhibited the significant DPP-IV inhibitory activity. Purification and identification led to the discovery of 387 peptide sequences. A total of 11 novel peptides with potential DPP-IV inhibitory activity were screened in silico. Further synthesis and validation of peptide activity showed that LTWR and DPF significantly inhibit DPP-IV in a competitive inhibitory manner, with IC50 values of 1788.67 ± 28.13 and 1399.73 ± 27.15 μM, respectively. Results from molecular docking and dynamic simulations indicated that peptides LTWR and DPF could tightly bind to the catalytic site of DPP-IV through hydrogen-bond and hydrophobic interaction. These findings suggested that Musculus senhousei could serve as a natural source of bioactive peptides for potential treatment of type 2 diabetes. |
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