A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates

The frequency (A), a novel in silico parameter, was developed by calculating the ratio of the number of truncated peptides with Xaa-proline and Xaa-alanine to all peptide fragments from a protein hydrolyzed with a specific protease.

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

Journal of Cereal Science ◽

10.1016/j.jcs.2015.07.004 ◽

2015 ◽

Vol 65 ◽

pp. 112-118 ◽

Cited By ~ 59

Author(s):

Alice B. Nongonierma ◽

Solène Le Maux ◽

Cécile Dubrulle ◽

Chloé Barre ◽

Richard J. FitzGerald

Keyword(s):

Antioxidant Properties ◽

Chenopodium Quinoa ◽

Dipeptidyl Peptidase ◽

Protein Hydrolysates ◽

Dipeptidyl Peptidase Iv ◽

Dpp Iv

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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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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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Quercetin and Coumarin Inhibit Dipeptidyl Peptidase-IV and Exhibits Antioxidant Properties: In Silico, In Vitro, Ex Vivo

Biomolecules ◽

10.3390/biom10020207 ◽

2020 ◽

Vol 10 (2) ◽

pp. 207 ◽

Cited By ~ 6

Author(s):

Anand-Krishna Singh ◽

Pankaj Kumar Patel ◽

Komal Choudhary ◽

Jaya Joshi ◽

Dhananjay Yadav ◽

...

Keyword(s):

Oxidative Stress ◽

In Silico ◽

Ex Vivo ◽

Antioxidant Properties ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Food Ingredients ◽

Dpp Iv ◽

In Silico Studies

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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Evaluation of some plants for potential dipeptidyl peptidase IV inhibitory effects in vitro

Turkish Journal of Biochemistry ◽

10.1515/tjb.2015.0004 ◽

2015 ◽

Vol 40 (3) ◽

Cited By ~ 1

Author(s):

Ali Zeytünlüoğlu ◽

Figen Zihnioğlu

Keyword(s):

Inhibitory Activity ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Vitis Vinifera L ◽

Aqueous Extracts ◽

Inhibitory Effects ◽

Dpp Iv ◽

Ic50 Values ◽

Glucagon Like Peptide 1

AbstractObjective: Dipeptidyl peptidase IV (DPP IV) is a serine amino (exo) peptidase which regulates various processes most notably plasma glucose homeostasis by cleaving incretin peptide hormones as glucagon-like peptide-1 (GLP-1) and glucose-dependent insulin releasing polypeptide (GIP). Realization of the inhibition of this enzyme in controlling diabetes is one of the strategies adopted in recent years. The present study was designed to investigate the DPP IV inhibitory effects of sixteen plant having antidiabetic property in aqueous extracts in correlation with their protein content.Methods: In vitro DPP IV inhibition was evaluated by the specific inhibitory activity of plant aqueous extracts prepared without and with heat (60°C) treatment.Results: Among the tested plants Vitis vinifera L., Artemisia dracunculus L., Prunus laurocerasus L., Rubus caesius L. and Olea europaea L. extracts showed DPP IV inhibitory activity with respect to IC50 values of 0.04-0.09 mg protein/ml. Kinetic analysis indicated that the inhibitor potency of A. dracunculus extract was stronger than the other extracts.Conclusion: The present study is the first report on screening and preliminary characterization of DPP IV inhibitory activity in aqueous extracts of selected antidiabetic medicinal food. This study could provide a new insight into DPP IV inhibitors from plants that could be useful for treatment of Type 2 diabetes.

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4-Hydroxyderricin Isolated from the Sap of Angelica keiskei Koidzumi: Evaluation of Its Inhibitory Activity towards Dipeptidyl Peptidase-IV

Scientia Pharmaceutica ◽

10.3390/scipharm87040030 ◽

2019 ◽

Vol 87 (4) ◽

pp. 30

Author(s):

Diah Lia Aulifa ◽

I Ketut Adnyana ◽

Jutti Levita ◽

Sukrasno Sukrasno

Keyword(s):

In Silico ◽

In Vitro Study ◽

Gradient Elution ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Inhibition Constant ◽

Hydroxyl Group ◽

Dpp Iv ◽

Angelica Keiskei

Angelica keiskei sap is used as a blood-sugar reducer in Indonesia, however its molecular mechanism has not yet been explored. 4-hydroxyderricin (4-HD) is one of the major components extracted from A. keiskei sap. The aim of this work was to isolate 4-HD from the sap of A. keiskei planted in Lombok, Indonesia, and to study in silico and in vitro mechanisms against dipeptidyl peptidase-IV (DPP-IV). The dried sap was submitted to liquid–liquid extraction using solvents with different polarity. Further purification processing was conducted using gradient elution column chromatography. The isolated compound was a yellowish powder, m/z 339.2215 [M + H]+, which was confirmed as 4-HD. Sitagliptin, a DPP-IV inhibitor, was employed as the positive control for both the in silico and in vitro studies. It was indicated that 4-HD interacts with Glu206 and Phe357, important amino acid residues in the DPP-IV binding pocket. These interactions are similar to that of sitagliptin. The affinity of 4-HD (inhibition constant (Ki) = 3.99 μM) to DPP-IV is lower than that of sitagliptin (inhibition constant (Ki) = 0.17 μM). Furthermore, in vitro study showed that 4-HD inhibits DPP-IV (IC50 = 81.44 μM) weaker than for sitagliptin (IC50 = 0.87 μM). We concluded that 4- HD might have potential in inhibiting DPP-IV. However, by considering the polar interaction of sitagliptin with DPP-IV, a further structure modification of 4-HD, e.g., by introducing a polar moiety such as a hydroxyl group, might be needed to obtain stronger activity as a DPP-IV inhibitor.

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