Next Article in Journal
Pharmacology of Herbal Sexual Enhancers: A Review of Psychiatric and Neurological Adverse Effects
Previous Article in Journal
Recent Progress of Chitosan and Chitosan Derivatives-Based Nanoparticles: Pharmaceutical Perspectives of Oral Insulin Delivery
Open AccessArticle

Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study

1
Department of Tropical Agriculture and International Cooperation, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
2
Department of Basic Science, Thainguyen University of Agriculture and Forestry, Quyetthang Ward, Thai Nguyen 250000, Vietnam
3
Department of Food Science, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
4
Department of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
5
International Master’s Degree Program in Food Science, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
6
Research Center for Animal Biologics, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan
*
Author to whom correspondence should be addressed.
Pharmaceuticals 2020, 13(10), 308; https://doi.org/10.3390/ph13100308
Received: 9 September 2020 / Revised: 30 September 2020 / Accepted: 13 October 2020 / Published: 14 October 2020
(This article belongs to the Section Biopharmaceuticals)
Five novel peptides (LPLF, WLQL, LPSW, VPGLAL, and LVGLPL) bearing dipeptidyl peptidase IV (DPP-IV) inhibitory activities were identified from the gastrointestinal enzymatic hydrolysate of soft-shelled turtle yolk (SSTY) proteins. Peptides were isolated separately using reversed-phase (RP) chromatography in parallel with off-line strong cation exchange (SCX) chromatography followed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis to determine sequences. Among these peptides, LPSW showed the highest DPP-IV inhibitory activity with an IC50 value of 269.7 ± 15.91 µM. The results of the pre-incubation experiment and the kinetic study of these peptides indicated that WLQL is a true inhibitor and its inhibition toward DPP-IV is of an uncompetitive model, while LPLF, LPSW, and VPGLAL are real-substrates and competitive inhibitors against DPP-IV. The DPP-IV inhibitory peptides derived from SSTY hydrolysate in study are promising in the management of hyperglycemia in Type 2 diabetes. View Full-Text
Keywords: DPP-IV inhibitory peptides; soft-shelled turtle yolk protein; bioassay-guided fractionation; LC-MS/MS; in silico analysis DPP-IV inhibitory peptides; soft-shelled turtle yolk protein; bioassay-guided fractionation; LC-MS/MS; in silico analysis
Show Figures

Graphical abstract

MDPI and ACS Style

Nong, N.T.P.; Chen, Y.-K.; Shih, W.-L.; Hsu, J.-L. Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study. Pharmaceuticals 2020, 13, 308.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop