scholarly journals Phycobiliproteins from Arthrospira Platensis (Spirulina): A New Source of Peptides with Dipeptidyl Peptidase-IV Inhibitory Activity

Nutrients ◽  
2020 ◽  
Vol 12 (3) ◽  
pp. 794 ◽  
Author(s):  
Yuchen Li ◽  
Gilda Aiello ◽  
Carlotta Bollati ◽  
Martina Bartolomei ◽  
Anna Arnoldi ◽  
...  
Keyword(s):  
Dose Response ◽  
Inhibitory Activity ◽  
Arthrospira Platensis ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Esi Ms ◽  
Dpp Iv ◽  
Ic50 Value ◽  
Metabolic Degradation

Arthrospira platensis (spirulina) is a cyanobacterium, which contains mainly two phycobiliproteins (PBP), i.e., C-phycocyanin (C-PC) and allophycocyanin (APC). In this study, PBP were hydrolyzed using trypsin, and the composition of the hydrolysate was characterized by HPLC-ESI-MS/MS. Furthermore, the potential anti-diabetic activity was assessed by using either biochemical or cellular techniques. Findings suggest that PBP peptides inhibit DPP-IV activity in vitro with a dose-response trend and an IC50 value falling in the range between 0.5 and 1.0 mg/mL. A lower inhibition of the DPP-IV activity expressed by Caco-2 cells was observed, which was explained by a secondary metabolic degradation exerted by the same cells.

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

2019 ◽  
Vol 20 (2) ◽  
pp. 322 ◽  
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.

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

2015 ◽  
Vol 40 (3) ◽  
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.

scholarly journals Characterization of Novel Dipeptidyl Peptidase-IV Inhibitory Peptides from Soft-Shelled Turtle Yolk Hydrolysate Using Orthogonal Bioassay-Guided Fractionations Coupled with In Vitro and In Silico Study

2020 ◽  
Vol 13 (10) ◽  
pp. 308
Author(s):  
Nhung Thi Phuong Nong ◽  
Yu-Kuo Chen ◽  
Wen-Ling Shih ◽  
Jue-Liang Hsu
Keyword(s):  
Dipeptidyl Peptidase ◽  
Reversed Phase ◽  
Dipeptidyl Peptidase Iv ◽  
Inhibitory Peptides ◽  
Dpp Iv ◽  
Ic50 Value ◽  
In Silico Study ◽  
Liquid Chromatography Tandem Mass

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.

scholarly journals IN VITRO ANTIDIABETIC EFFECTS OF FERULA ASSA-FOETIDA EXTRACTS THROUGH DIPEPTIDYL PEPTIDASE IV AND α-GLUCOSIDASE INHIBITORY ACTIVITY

2017 ◽  
Vol 10 (5) ◽  
pp. 357 ◽  
Author(s):  
Adel Yarizade ◽  
Hsan Hasani Kumle ◽  
Ali Niazi
Keyword(s):  
Diabetes Mellitus ◽  
Inhibitory Activity ◽  
Postprandial Glucose ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Dpp Iv ◽  
Glucosidase Inhibitors ◽  
Treatment Of Diabetes ◽  
Ethanol Ethanol

Objective: Diabetes mellitus (DM) causes hyperglycemia, which is one of the most common diseases in the world. One of the strategies for the treatment of diabetes is maintaining postprandial glucose level through inhibition of dipeptidyl peptidase IV (DPP-IV) and α-glucosidase enzymes. The aim of this study was to determine in vitro antidiabetic potential of Ferula assa-foetida via DPP-IV and α-glucosidase inhibitory activities.Methods: F. assa-foetida seeds were extracted in methanol, ethanol, ethanol-methanol, and water. Inhibitory activity on DPP-IV and α-glucosidase wasperformed in vitro and measured spectrophotometrically at λ=405 nm.Results: The result showed that the F. assa-foetida seed extract is effective against both enzymes. All fractions had DPP-IV inhibitory activity, but the ethanolic fraction had the highest inhibitory activity on DPP-IV enzyme and significantly decreased DPP-IV activity (24.5%). With respect to α-glucosidase inhibitory activity, the aqueous extract has the highest inhibitory activity (28%).Conclusion: According to the results of this study, F. assa-foetida contains DPP-IV and α-glucosidase inhibitors and could be a potential source for the discovery of active constituents as α-glucosidase and DPP-IV inhibitors to treat Type 2 DM.Keywords: Diabetes mellitus, Herbal medicine, Dipeptidyl peptidase IV, α-glucosidase.

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

2020 ◽  
Vol 131 ◽  
pp. 108989 ◽  
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

scholarly journals Natural phenolic compounds potentiate hypoglycemia via inhibition of Dipeptidyl peptidase IV

2019 ◽  
Vol 9 (1) ◽  
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.

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

2006 ◽  
Vol 52 (1) ◽  
pp. 82-87 ◽  
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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