scholarly journals Generation of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides during the enzymatic hydrolysis of tropical banded cricket (Gryllodes sigillatus) proteins

2018 ◽  
Vol 9 (1) ◽  
pp. 407-416 ◽  
Author(s):  
Alice B. Nongonierma ◽  
Candice Lamoureux ◽  
Richard J. FitzGerald

Cricket (Gryllodes sigillatus) protein hydrolysates inhibit dipeptidyl peptidase IV (DPP-IV) in vitro.

2015 ◽  
Vol 65 ◽  
pp. 112-118 ◽  
Author(s):  
Alice B. Nongonierma ◽  
Solène Le Maux ◽  
Cécile Dubrulle ◽  
Chloé Barre ◽  
Richard J. FitzGerald

2019 ◽  
Vol 20 (2) ◽  
pp. 322 ◽  
Author(s):  
Yating Lu ◽  
Peng Lu ◽  
Yu Wang ◽  
Xiaodong Fang ◽  
Jianming Wu ◽  
...  

Dipeptidyl peptidase IV (DPP-IV) inhibitors occupy a growing place in the drugs used for the management of type 2 diabetes. Recently, food components, including food-derived bioactive peptides, have been suggested as sources of DPP-IV inhibitors without side effects. Chinese black tea is a traditional health beverage, and it was used for finding DPP-IV inhibitory peptides in this study. The ultra-filtrated fractions isolated from the aqueous extracts of black tea revealed DPP-IV inhibitory activity in vitro. Four peptides under 1 kDa were identified by SDS-PAGE and LC-MS/MS (Liquid Chromatography-Mass Spectrometry-Mass Spectrometry) from the ultra-filtrate. The peptide II (sequence: AGFAGDDAPR), with a molecular mass of 976 Da, showed the greatest DPP-IV inhibitory activity (in vitro) among the four peptides. After administration of peptide II (400 mg/day) for 57 days to streptozotocin (STZ)-induced hyperglycemic mice, the concentration of glucagon-like peptide-1 (GLP-1) in the blood increased from 9.85 ± 1.96 pmol/L to 19.22 ± 6.79 pmol/L, and the insulin level was increased 4.3-fold compared to that in STZ control mice. Immunohistochemistry revealed the improved function of pancreatic beta-cells and suppressed proliferation of pancreatic alpha-cells. This study provides new insight into the use of black tea as a potential resource of food-derived DPP-IV inhibitory peptides for the management of type 2 diabetes.


2020 ◽  
Vol 13 (10) ◽  
pp. 308
Author(s):  
Nhung Thi Phuong Nong ◽  
Yu-Kuo Chen ◽  
Wen-Ling Shih ◽  
Jue-Liang Hsu

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.


2021 ◽  
Author(s):  
Fernando Rivero-Pino ◽  
Antonio Guadix ◽  
Emilia M. Guadix

Enzymatic hydrolysis improved the antidiabetic activity of Tenebrio molitor protein. Peptides below 2000 Da were the most bioactive. Some novel peptides were identified to be DPP-IV and α-glucosidase inhibitors.


2013 ◽  
Vol 73 (1) ◽  
pp. 34-46 ◽  
Author(s):  
Orla Power ◽  
A. B. Nongonierma ◽  
P. Jakeman ◽  
R. J. FitzGerald

The prevalence of type 2 diabetes mellitus (T2DM) is increasing and it is estimated that by 2030 approximately 366 million people will be diagnosed with this condition. The use of dipeptidyl peptidase IV (DPP-IV) inhibitors is an emerging strategy for the treatment of T2DM. DPP-IV is a ubiquitous aminodipeptidase that cleaves incretins such as glucagon like peptide 1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), resulting in a loss in their insulinotropic activity. Synthetic DPP-IV drug inhibitors are being used to increase the half-life of the active GLP-1 and GIP. Dietary intervention is accepted as a key component in the prevention and management of T2DM. Therefore, identification of natural food protein-derived DPP-IV inhibitors is desirable. Peptides with DPP-IV inhibitory activity have been identified in a variety of food proteins. This review aims to provide an overview of food protein hydrolysates as a source of the DPP-IV inhibitory peptides with particular focus on milk proteins. In addition, the proposed modes of inhibition and structure–activity relationship of peptide inhibitors are discussed. Milk proteins and associated peptides also display insulinotropic activity and help regulate blood glucose in healthy and diabetic subjects. Therefore, milk protein derived peptide inhibitors may be a unique multifunctional peptide approach for the management of T2DM.


2018 ◽  
Vol 244 ◽  
pp. 340-348 ◽  
Author(s):  
Alice B. Nongonierma ◽  
Sara Paolella ◽  
Priti Mudgil ◽  
Sajid Maqsood ◽  
Richard J. FitzGerald

2017 ◽  
Vol 94 ◽  
pp. 79-89 ◽  
Author(s):  
Alice B. Nongonierma ◽  
Caterina Mazzocchi ◽  
Sara Paolella ◽  
Richard J. FitzGerald

2017 ◽  
Vol 8 (6) ◽  
pp. 2249-2257 ◽  
Author(s):  
A. B. Nongonierma ◽  
M. Hennemann ◽  
S. Paolella ◽  
R. J. FitzGerald

Wheat gluten hydrolysates contain known/potential DPP-IV inhibitory peptides.


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