Release of dipeptidyl peptidase IV inhibitory peptides from salmon (Salmo salar) skin collagen based on digestion-intestinal absorption in vitro
文献类型： 外文期刊
作者： Ritian, Jin 1 ; Teng, Xiangyu 1 ; Liao, Minhe 1 ; Zhang, Ligang 1 ; Wei, Zikai 1 ; Meng, Ran 3 ; Liu, Ning 1 ;
作者机构： 1.Northeast Agr Univ, Coll Food Sci, Harbin 150030, Peoples R China
2.Northeast Agr Univ, Key Lab Dairy Sci, Minist Educ, Harbin 150030, Peoples R China
3.Hebei Acad Agr & Forestry Sci, Binhai Agr Res Inst, Tangshan Key Lab Plant Salt Tolerance Res, Tangshan 063200, Peoples R China
关键词： Caco‐ 2 cells; dipeptidyl peptidase IV; inhibitory peptide; molecular docking; salmon skin collagen; type 2 diabetes
期刊名称：INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY （ 影响因子：2.773； 五年影响因子：2.516 ）
ISSN： 0950-5423
年卷期：
页码：
收录情况： SCI
摘要： Inhibition of dipeptidyl peptidase IV (DPP-IV) was considered to be a crucial target for type 2 diabetes, and food-derived peptides were superior source of DPP-IV inhibitory peptides. The purpose of this investigation was to identify inhibitory peptides from salmon skin collagen using simulated digestion combined with Caco-2 cell monolayer membrane model. The analysis in silico showed that TKLPAVF and YLNF were potential inhibitory peptides. Determination of the inhibition activity showed that the IC50 values of TKLPVAF and YLNF were 242.10 +/- 3.40 and 146.90 +/- 4.40 mu m, respectively. Molecular docking results showed that seven hydrogen bonds were formed between YLNF and key residues of DPP-IV. YLNF may be considered a novel DPP-IV inhibitory peptide. In addition, YLNF could be transported by Caco-2 cell monolayer membrane in intact, and the apparent permeability coefficient value was (3.54 +/- 0.34) x 10(-6) cm s(-1) at 5 mm.
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