دورية أكاديمية

Identification, rapid screening, docking mechanism and in vitro digestion stability of novel DPP-4 inhibitory peptides from wheat gluten with ginger protease.

التفاصيل البيبلوغرافية
العنوان: Identification, rapid screening, docking mechanism and in vitro digestion stability of novel DPP-4 inhibitory peptides from wheat gluten with ginger protease.
المؤلفون: Pu L; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Kong X; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Xing R; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Wang Y; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Zhang C; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Hua Y; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Chen Y; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China., Li X; State Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, P. R. China. xzkong@jiangnan.edu.cn.; School of Food Science and Technology, Jiangnan University, Wuxi, P. R. China.
المصدر: Food & function [Food Funct] 2024 Apr 02; Vol. 15 (7), pp. 3848-3863. Date of Electronic Publication: 2024 Apr 02.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 101549033 Publication Model: Electronic Cited Medium: Internet ISSN: 2042-650X (Electronic) Linking ISSN: 20426496 NLM ISO Abbreviation: Food Funct Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge : Royal Society of Chemistry
مواضيع طبية MeSH: Diabetes Mellitus, Type 2*/drug therapy , Dipeptidyl-Peptidase IV Inhibitors*/chemistry , Plant Proteins* , Cysteine Proteases*, Triticum/chemistry ; Tandem Mass Spectrometry ; Hydrolysis ; Peptides/chemistry ; Glutens ; Digestion ; Dipeptidyl Peptidase 4/chemistry
مستخلص: To better understand the hypoglycemic potential of wheat gluten (WG), we screened dipeptidyl peptidase IV (DPP-4) inhibitory active peptides from WG hydrolysates. WG hydrolysates prepared by ginger protease were found to have the highest DPP-4 inhibitory activity among the five enzymatic hydrolysates, from which a 1-3 kDa fraction was isolated by ultrafiltration. Further characterization of the fraction with nano-HPLC-MS/MS revealed 1133 peptides. Among them, peptides with P' 2 (the second position of the N-terminal) and P 2 (the second position of the C-terminal) as proline residues (Pro) accounted for 12.44% and 43.69%, respectively. The peptides including Pro-Pro-Phe-Ser (PPFS), Ala-Pro-Phe-Gly-Leu (APFGL), and Pro-Pro-Phe-Trp (PPFW) exhibited the most potent DPP-4 inhibitory activity with IC 50 values of 56.63, 79.45, and 199.82 μM, respectively. The high inhibitory activity of PPFS, APFGL, and PPFW could be mainly attributed to their interaction with the S2 pocket (Glu205 and Glu206) and the catalytic triad (Ser630 and His740) of DPP-4, which adopted competitive, mixed, and mixed inhibitory modes, respectively. After comparative analysis of PPFS, PPFW, and PPF, Ser was found to be more conducive to enhancing the DPP-4 inhibitory activity. Interestingly, peptides with P 2 as Pro also exhibited good DPP-4 inhibitory activity. Meanwhile, DPP-4 inhibitory peptides from WG showed excellent stability, suggesting a potential application in type 2 diabetes (T2DM) therapy or in the food industry as functional components.
المشرفين على المادة: EC 3.4.22.67 (zingipain, Zingiber officinale)
0 (Dipeptidyl-Peptidase IV Inhibitors)
0 (Peptides)
8002-80-0 (Glutens)
EC 3.4.14.5 (Dipeptidyl Peptidase 4)
0 (Plant Proteins)
EC 3.4.- (Cysteine Proteases)
تواريخ الأحداث: Date Created: 20240321 Date Completed: 20240403 Latest Revision: 20240403
رمز التحديث: 20240403
DOI: 10.1039/d3fo05423c
PMID: 38512162
قاعدة البيانات: MEDLINE
الوصف
تدمد:2042-650X
DOI:10.1039/d3fo05423c