Journal
MOLECULES
Volume 22, Issue 10, Pages -Publisher
MDPI AG
DOI: 10.3390/molecules22101714
Keywords
bioactive peptide; dipeptidyl peptidase-IV; identification; molecular docking; nano-LC-MS/MS; Ruditapes philippinarum
Funding
- Priority Academic Program Development of the Jiangsu Higher Education Institutions (PAPD)
- State Ocean Administration of China [201305007, 201405017]
- Jiangsu Social Science Fund [5ZXC004]
- Jiangsu Qinlan Project
- Jiangsu 333 Project
- Jiangsu Science and Technology Research Funds [17KJA360005]
- Jiangsu Marine Technological Innovation Project [HY2017-7]
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Dipeptidyl peptidase-IV (DPP-IV) inhibitory peptides were rapidly identified from Ruditapes philippinarum hydrolysate. The hydrolysate was fractionated by ethanol precipitation and preparative reverse phase high-performance liquid chromatography (RP-HPLC). The fraction which showed the highest DPP-IV inhibitory activity was then analyzed by a high-throughput nano-liquid chromatography electrospray ionization tandem mass spectrometry (nano-LC ESI-MS/MS) method, and the sequences of peptides were identified based on the MS/MS spectra against the Mollusca protein data from the UniProt database. In total, 50 peptides were identified. Furthermore, molecular docking was used to identify potential DPP-IV inhibitors from the identified peptides. Docking results suggested that four peptides: FAGDDAPR, LAPSTM, FAGDDAPRA, and FLMESH, could bind pockets of DPP-IV through hydrogen bonds, pi-pi bonds, and charge interactions. The four peptides were chemically synthesized and tested for DPP-IV inhibitory activity. The results showed that they possessed DPP-IV inhibitory activity with IC50 values of 168.72 mu M, 140.82 mu M, 393.30 mu M, and >500 mu M, respectively. These results indicate that R. philippinarum-derived peptides may have potential as functional food ingredients for the prevention of diabetes.
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