期刊
PHARMACEUTICALS
卷 13, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/ph13100308
关键词
DPP-IV inhibitory peptides; soft-shelled turtle yolk protein; bioassay-guided fractionation; LC-MS/MS; in silico analysis
资金
- Ministry of Science and Technology [MOST 109-2634-F-020-001]
- Animal Biologics Research of the Featured Area Research Center within Ministry of Education
- Animal Biologics Research of the Featured Area Research Center within Ministry of Science and Technology, Taiwan [MOST 109-2634-F-020-001]
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 mu M. 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.
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