Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties

Quercetin and coumarin, two naturally occurring phytochemicals of plant origin, are known to regulate hyperglycemia and oxidative stress. The present study was designed to evaluate the inhibitory activity of quercetin and coumarin on dipeptidyl peptidase-IV (DPP-IV) and their antioxidant potential. DPP-IV inhibition assays were performed, and evaluated IC50 values of diprotin A, quercetin, coumarin, and sitagliptin were found to be 0.653, 4.02, 54.83, and 5.49 nmol/mL, respectively. Furthermore, in silico studies such as the drug-likeliness and docking efficiency of quercetin and coumarin to the DPP-IV protein were performed; the ex vivo antiperoxidative potential of quercetin and coumarin were also evaluated. The results of the present study showed that the DPP-IV inhibitory potential of quercetin was slightly higher than that of sitagliptin. Virtual docking revealed the tight binding of quercetin with DPP-IV protein. Quercetin and coumarin reduced oxidative stress in vitro and ex vivo systems. We report for the first time that both compounds inhibited the DPP-IV along with antioxidant activity and thus may be use as function food ingredients in the prevention of diabetes.

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

Food & Function ◽

10.1039/c7fo01568b ◽

2018 ◽

Vol 9 (1) ◽

pp. 407-416 ◽

Cited By ~ 13

Author(s):

Alice B. Nongonierma ◽

Candice Lamoureux ◽

Richard J. FitzGerald

Keyword(s):

Enzymatic Hydrolysis ◽

Dipeptidyl Peptidase ◽

Protein Hydrolysates ◽

Dipeptidyl Peptidase Iv ◽

Inhibitory Peptides ◽

Dpp Iv ◽

Gryllodes Sigillatus ◽

Hydrolysis Of

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

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Identification and characterisation of peptides from a boarfish (Capros aper) protein hydrolysate displaying in vitro dipeptidyl peptidase-IV (DPP-IV) inhibitory and insulinotropic activity

Food Research International ◽

10.1016/j.foodres.2020.108989 ◽

2020 ◽

Vol 131 ◽

pp. 108989 ◽

Cited By ~ 6

Author(s):

Pádraigín A. Harnedy-Rothwell ◽

Chris M. McLaughlin ◽

Martina B. O'Keeffe ◽

Aurélien V. Le Gouic ◽

Philip J. Allsopp ◽

...

Keyword(s):

Protein Hydrolysate ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Dpp Iv

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Natural phenolic compounds potentiate hypoglycemia via inhibition of Dipeptidyl peptidase IV

Scientific Reports ◽

10.1038/s41598-019-52088-7 ◽

2019 ◽

Vol 9 (1) ◽

Cited By ~ 5

Author(s):

Po-Kai Huang ◽

Shian-Ren Lin ◽

Chia-Hsiang Chang ◽

May-Jwan Tsai ◽

Der-Nan Lee ◽

...

Keyword(s):

Phenolic Compounds ◽

Blood Sugar ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

C2c12 Cells ◽

Surface Glycoprotein ◽

Dpp Iv ◽

Natural Phenolic Compounds

Abstract Dipeptidyl peptidase IV (DPP IV) is a surface glycoprotein that can degrade glucagon like pepetide-1 (GLP-1) by decreasing blood sugar. Herbal medicines for diabetic therapy are widely used with acceptable efficacy but unsatisfied in advances. DPP IV was chosen as a template to employ molecular docking via Discovery Studio to search for natural phenolic compounds whether they have the inhibitory function of DPP IV. Then, docking candidates were validated and further performed signal pathway via Caco-2, C2C12, and AR42J cells. Lastly, a diet-induced diabetes in mice were applied to examine the efficacy and toxicity of hit natural phenolic products in long-term use (in vivo). After screening, curcumin, syringic acid, and resveratrol were found in high affinity with DPP IV enzymes. In enzymatic tests, curcumin and resveratrol showed potential inhibition of DPP IV. In vitro assays, curcumin inhibited of DPP IV activity in Caco-2 cells and ERK phosphorylation in C2C12 cells. Additionally, curcumin attenuated blood sugar in S961-treated C57BL/6 mice and in diet-induced diabetic ICR mice and long-term regulate HbA1c in diabetic mice. Curcumin targeted to DPP IV for reducing blood glucose, it possesses potential and alternative substitution of synthetic clinical drugs for the medication of diabetes.

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Dipeptidyl-Peptidase IV Converts Intact B-Type Natriuretic Peptide into Its des-SerPro Form

Clinical Chemistry ◽

10.1373/clinchem.2005.057638 ◽

2006 ◽

Vol 52 (1) ◽

pp. 82-87 ◽

Cited By ~ 145

Author(s):

Inger Brandt ◽

Anne-Marie Lambeir ◽

Jean-Marie Ketelslegers ◽

Marc Vanderheyden ◽

Simon Scharpé ◽

...

Keyword(s):

Natriuretic Peptide ◽

Ex Vivo ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Dependent Manner ◽

Concentration Dependent Manner ◽

Amino Terminal ◽

Dpp Iv

Abstract Background: Analysis of plasma B-type natriuretic peptide (BNP) has suggested the in vivo formation of a truncated form, BNP (3–32), also called des-SerPro-BNP. The objectives of this study were to investigate (a) whether BNP and other natriuretic peptides are truncated by dipeptidyl-peptidase IV (DPP IV/CD26; EC 3.4.14.5) and (b) whether this truncation affects the susceptibility to cleavage by neutral endopeptidase (NEP; EC 3.4.24.11). Methods: Human BNP (1–32), A-type natriuretic peptide 1–28 (ANP 1–28), and related peptides were incubated with purified DPP IV and with human plasma. In addition, BNP (1–32), BNP (3–32), and ANP (1–28) were subjected to hydrolysis by NEP. Cleavage products were analyzed by mass spectrometry. Results: BNP (1–32) was cleaved by purified DPP IV with a specificity constant of 0.37 × 106 L · mol−1 · s−1. The DPP IV activity in EDTA-plasma was able to truncate BNP (1–32) ex vivo. Addition of Vildagliptin, a specific DPP IV inhibitor, prevented this truncation in a concentration-dependent manner. Under in vitro circumstances in which ANP was hydrolyzed extensively, BNP (1–32) and BNP (3–32) were very resistant to NEP-mediated cleavage. Conclusions: DPP IV cleaves BNP (1–32) with an efficiency higher than or comparable to several known in vivo substrates of the enzyme. Even after loss of the amino-terminal dipeptide, BNP remains highly resistant to cleavage by NEP.

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In vitro α-glucosidase, angiotensin converting enzyme and dipeptidyl peptidase-IV inhibitory properties of brewers' spent grain protein hydrolysates

Food Research International ◽

10.1016/j.foodres.2013.12.021 ◽

2014 ◽

Vol 56 ◽

pp. 100-107 ◽

Cited By ~ 42

Author(s):

Alan Connolly ◽

Charles O. Piggott ◽

Richard J. FitzGerald

Keyword(s):

Angiotensin Converting Enzyme ◽

Dipeptidyl Peptidase ◽

Protein Hydrolysates ◽

Dipeptidyl Peptidase Iv ◽

Grain Protein ◽

Converting Enzyme ◽

Spent Grain

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Generation of Dipeptidyl Peptidase-IV-Inhibiting Peptides fromβ-Lactoglobulin Secreted byLactococcus lactis

BioMed Research International ◽

10.1155/2014/393598 ◽

2014 ◽

Vol 2014 ◽

pp. 1-8 ◽

Cited By ~ 9

Author(s):

Suguru Shigemori ◽

Kazushi Oshiro ◽

Pengfei Wang ◽

Yoshinari Yamamoto ◽

Yeqin Wang ◽

...

Keyword(s):

Diabetes Mellitus ◽

Type 2 Diabetes ◽

Expression System ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Delivery Vehicle ◽

Dpp Iv

Previous studies showed that hydrolysates ofβ-lactoglobulin (BLG) prepared using gastrointestinal proteases strongly inhibit dipeptidyl peptidase-IV (DPP-IV) activityin vitro. In this study, we developed a BLG-secretingLactococcus lactisstrain as a delivery vehicle andin situexpression system. Interestingly, trypsin-digested recombinant BLG fromL. lactisinhibited DPP-IV activity, suggesting that BLG-secretingL. lactismay be useful in the treatment of type 2 diabetes mellitus.

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A Novel Dipeptidyl Peptidase IV Inhibitory Tea Peptide Improves Pancreatic β-Cell Function and Reduces α-Cell Proliferation in Streptozotocin-Induced Diabetic Mice

International Journal of Molecular Sciences ◽

10.3390/ijms20020322 ◽

2019 ◽

Vol 20 (2) ◽

pp. 322 ◽

Cited By ~ 3

Author(s):

Yating Lu ◽

Peng Lu ◽

Yu Wang ◽

Xiaodong Fang ◽

Jianming Wu ◽

...

Keyword(s):

Mass Spectrometry ◽

Type 2 Diabetes ◽

Inhibitory Activity ◽

Black Tea ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Inhibitory Peptides ◽

Dpp Iv

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.

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Bioactive Peptides from Germinated Soybean with Anti-Diabetic Potential by Inhibition of Dipeptidyl Peptidase-IV, α-Amylase, and α-Glucosidase Enzymes

International Journal of Molecular Sciences ◽

10.3390/ijms19102883 ◽

2018 ◽

Vol 19 (10) ◽

pp. 2883 ◽

Cited By ~ 22

Author(s):

Marcela González-Montoya ◽

Blanca Hernández-Ledesma ◽

Rosalva Mora-Escobedo ◽

Cristina Martínez-Villaluenga

Keyword(s):

Soybean Protein ◽

Dipeptidyl Peptidase ◽

Structural Features ◽

Protein Isolate ◽

Dipeptidyl Peptidase Iv ◽

Dpp Iv ◽

Phase Liquid ◽

Peptide Fractions ◽

Germinated Soybean

Functional foods containing peptides offer the possibility to modulate the absorption of sugars and insulin levels to prevent diabetes. This study investigates the potential of germinated soybean peptides to modulate postprandial glycaemic response through inhibition of dipeptidyl peptidase IV (DPP-IV), salivary α-amylase, and intestinal α-glucosidases. A protein isolate from soybean sprouts was digested by pepsin and pancreatin. Protein digest and peptide fractions obtained by ultrafiltration (<5, 5–10 and >10 kDa) and subsequent semipreparative reverse phase liquid chromatography (F1, F2, F3, and F4) were screened for in vitro inhibition of DPP-IV, α-amylase, maltase, and sucrase activities. Protein digest inhibited DPP-IV (IC50 = 1.49 mg/mL), α-amylase (IC50 = 1.70 mg/mL), maltase, and sucrase activities of α-glucosidases (IC50 = 3.73 and 2.90 mg/mL, respectively). Peptides of 5–10 and >10 kDa were more effective at inhibiting DPP-IV (IC50 = 0.91 and 1.18 mg/mL, respectively), while peptides of 5–10 and <5 kDa showed a higher potency to inhibit α-amylase and α-glucosidases. Peptides in F1, F2, and F3 were mainly fragments from β-conglycinin, glycinin, and P34 thiol protease. The analysis of structural features of peptides in F1–F3 allowed the tentative identification of potential antidiabetic peptides. Germinated soybean protein showed a promising potential to be used as a nutraceutical or functional ingredient for diabetes prevention.

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In vitro dipeptidyl peptidase IV inhibitory activity and in situ insulinotropic activity of milk and egg white protein digests

Food & Function ◽

10.1039/d1fo00641j ◽

2021 ◽

Author(s):

Marta Santos-Hernandez ◽

Maria Cermeno ◽

Isidra Recio ◽

Richard J. FitzGerald

Keyword(s):

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Food Protein ◽

Protein Digestion ◽

Egg White Protein ◽

Dpp Iv ◽

Protein Digests ◽

Incretin Secretion

Dietary proteins are involved in the regulation of glucose homeostasis by different mechanisms. Food protein digestion products are reported to inhibit dipeptidyl peptidase IV (DPP-IV), induce incretin secretion or directly...

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