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Molecules 2017, 22(10), 1714; doi:10.3390/molecules22101714

Rapid Identification of Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Peptides from Ruditapes philippinarum Hydrolysate

1,2,3,†,* , 4,†
,
5
,
1,2
,
1,2
,
1,2
,
1,2
and
1,2,*
1
Jiangsu Key Laboratory of Research and Development in Marine Bio-Resource Pharmaceutics, Nanjing University of Chinese Medicine, Nanjing 210023, China
2
College of Pharmacy, Nanjing University of Chinese Medicine, Nanjing 210023, China
3
Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing 210023, China
4
The Affiliated Huai’an of Xuzhou Medical College and The Second People’s Hospital of Huai’an, Huai’an 223002, China
5
Nanjing Normal University, School of Public Administration, Nanjing 210023, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Received: 30 August 2017 / Revised: 8 October 2017 / Accepted: 9 October 2017 / Published: 13 October 2017
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Abstract

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, π-π 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 μM, 140.82 μM, 393.30 μM, and >500 μM, respectively. These results indicate that R. philippinarum-derived peptides may have potential as functional food ingredients for the prevention of diabetes. View Full-Text
Keywords: bioactive peptide; dipeptidyl peptidase-IV; identification; molecular docking; nano-LC-MS/MS; Ruditapes philippinarum bioactive peptide; dipeptidyl peptidase-IV; identification; molecular docking; nano-LC-MS/MS; Ruditapes philippinarum
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MDPI and ACS Style

Liu, R.; Zhou, L.; Zhang, Y.; Sheng, N.-J.; Wang, Z.-K.; Wu, T.-Z.; Wang, X.-Z.; Wu, H. Rapid Identification of Dipeptidyl Peptidase-IV (DPP-IV) Inhibitory Peptides from Ruditapes philippinarum Hydrolysate. Molecules 2017, 22, 1714.

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