<i>In Silico</i>Evaluation of Potential DPP-III Inhibitor Precursors from Dietary Proteins

Khaket, Tejinder Pal; Redhu, Davender; Dhanda, Suman; Singh, Jasbir

doi:10.1080/10942912.2013.787626

Cited by 16 publications

(7 citation statements)

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“…These opioid peptides regulate diverse physiological functions such as signal transduction, gastrointestinal motility, immune and endocrine functions, and mostly pain modulation. Dipeptides with aromatic residues such as YY, YF, and containing large aliphatic or basic amino acids have been described as potent inhibitors (Khaket et al 2015). Few studies have identified DPP III inhibitory peptides from meat proteins, however, hemoglobin could present a high potential as source of such bioactive peptides (Khaket et al 2015).…”

Section: Bioactivity Of Dipeptides and Tripeptidesmentioning

confidence: 99%

“…Dipeptides with aromatic residues such as YY, YF, and containing large aliphatic or basic amino acids have been described as potent inhibitors (Khaket et al 2015). Few studies have identified DPP III inhibitory peptides from meat proteins, however, hemoglobin could present a high potential as source of such bioactive peptides (Khaket et al 2015). In dry-cured hams, creatine kinase-derived dipeptides such as HK, HP, and LA would show DPP III inhibitory activity according to the BIOPEP database ( Table 3).…”

Section: Bioactivity Of Dipeptides and Tripeptidesmentioning

confidence: 99%

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The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham

Gallego

Mora

Toldrá

2019

Food Prod Process and Nutr

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Dry-cured ham has been described as a good source of bioactive peptides and taste-active compounds. Some of them are dipeptides and tripeptides that are released in a large amount from different muscle proteins due to the action of exopeptidases during the dry-cured ham processing. The potential of dipeptides and tripeptides to exert bioactivities and impart taste characteristics to dry-cured ham has been evaluated using the BIOPEP database, since in silico approaches are a time-and cost-effective alternative to empirical approaches. Most of the studied dipeptides and tripeptides showed ACE and DPP inhibitory activities as well as imparted bitter taste. In fact, more than one bioactivity and/or taste could be assigned to a given peptide sequence, and there could be a correlation between both, like ACE inhibitory and bitter EA, EI and LG peptides. Furthermore, several dipeptides such as EK, KP, LA, PL, PP, RG, and VE, among others, were found to be multifunctional (ACE and DPP IV inhibitory) which would be determined by their structure, sequence and amino acid composition. In silico analysis evidences the relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured hams, but further empirical assays including in vitro and in vivo studies are necessary to confirm such theoretical results. Possible degradation of the small peptides during gastrointestinal digestion and intestinal absorption as well as interactions with the food matrix could reduce their bioavailability and bioaccessibility, and modify their biological activities.

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Section: Bioactivity Of Dipeptides and Tripeptidesmentioning

confidence: 99%

Section: Bioactivity Of Dipeptides and Tripeptidesmentioning

confidence: 99%

The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham

Gallego

Mora

Toldrá

2019

Food Prod Process and Nutr

View full text Add to dashboard Cite

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“…According to the report by Khaket et al [ 53 ], the β-subunit of chicken hemoglobin and annexin A5 showed a high inhibitory potential for DPP-III in in silico studies. However, as noted by Galleo et al [ 16 ], only a few studies identified peptides that inhibit DPP-III from meat proteins.…”

Section: Resultsmentioning

confidence: 99%

Peptides from Different Carcass Elements of Organic and Conventional Pork—Potential Source of Antioxidant Activity

Kęska

Rohn²,

Halagarda

et al. 2020

Antioxidants

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The growing consumer interest in organic foods, as well as, in many cases, the inconclusiveness of the research comparing organic and conventional foods, indicates a need to study this issue further. The aim of the study was to compare the effects of meat origin (conventional vs. organic) and selected elements of the pork carcass (ham, loin, and shoulder) on the meat proteome and the antioxidant potential of its peptides. The peptidomic approach was used, while the ability of antioxidants to scavenge 2,2′-azino-bis-3-ethylbenzthiazoline-6-sulfonic acid (ABTS), to chelate Fe(II) ions, and to reduce Fe(III) was determined. Most peptides were derived from myofibrillary proteins. The meat origin and the element of the pork carcass did not have a significant effect on the proteome. On the other hand, the pork origin and the carcass element significantly affected the iron ion-chelating capacity (Fe(II)) and the reducing power of peptides. In particular, pork ham from conventional rearing systems had the best antioxidant properties in relation to potential antioxidant peptides. This could be a factor for human health, as well as for stabilized meat products (e.g., toward lipid oxidation).

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“…This study was correlated with an earlier investigation, which was determined the dipeptidyl peptidase IV inhibitory activity of protein hydrolysates from tropical banded cricket 27 , salmon skin gelatin hydrolysates 50 , and quinoa protein hydrolysates 51 . This investigation is not surprising task since most peptides are identified as di-or tri-peptides and described to have dipeptidyl peptidase IV inhibitory activity 52,53 .…”

Section: Discussionmentioning

confidence: 97%

Untitled

2020

IJPSR

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The bioactive peptides derived from food have increased consideration for their function in averting numerous chronic diseases, comprising, diabetes and obesity. Edible insects are the feasible composition of bioactive peptides owing to their high protein content and viable production. The present study was aimed to evaluate the antidiabetic and anti-obesity effects of seven edible insects' protein hydrolysates after simulated gastrointestinal enzymatic digestion. Antidiabetic and anti-obesity efficiency was determined by the inhibition of digestive enzymes viz., dipeptidyl peptidase-IV, α-glucosidase, and α-lipase activity. Three active protein hydrolysate extracts (1.25, 2.5, and 5mg/dl) were selected and analyzed in terms of their IC 50 values, and all tested extracts inhibited those enzyme activities in a dose-dependent manner. Based on the present study, we conclude the seven edible insects' hydrolysate have potential enzyme inhibitory activities and thereby proved as an antidiabetic and anti-obesity activity. INTRODUCTION: Diabetes Mellitus is wellknown metabolic syndromes measured by high blood glucose and failings of insulin synthesis or insulin action, or both, which may cause serious complications, including retinopathy, nephropathy, neuropathy, obesity, and cardiovascular diseases 1-3. Diabetes and its hitches have established significant attention due to augmented health menaces, and its treatment costs 4, 5. The number of individuals suffering from diabetes and obesity has been tripled since 1990 and becomes the main challenge for our society globally 6, 7. Diabetes with overweight and obesity are the foremost risk factors for numerous chronic diseases, including cardiovascular diseases and various cancers 8-10 .

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In SilicoEvaluation of Potential DPP-III Inhibitor Precursors from Dietary Proteins

Cited by 16 publications

References 36 publications

The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham

The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham

Peptides from Different Carcass Elements of Organic and Conventional Pork—Potential Source of Antioxidant Activity

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