Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Nongonierma, Alice B.; Fitzgerald, Richard J.

doi:10.1039/c3fo60262a

Cited by 74 publications

(58 citation statements)

References 36 publications

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“…However, in other instances, free W antioxidant activity was as high as that of W-containing peptides such as with the oxygen radical absorbance capacity (ORAC) assay and with XO 30 inhibition (Table 5). In addition, the peptide sequence also affected the antioxidant activity as demonstrated in studies conducted with reverse peptides 79,82,83 or when substituting amino acids in peptides 74 . It is interesting to note that certain peptides yielded good antioxidant properties across different 35 assays (Table 5).…”

Section: Article Type Wwwrscorg/xxxxxx | Xxxxxxxxmentioning

confidence: 99%

“…It was shown with dipeptide isomers that DPP-IV inhibitory activity was significantly reduced or lost when the W residue was located at 30 the C-terminal position of the peptide 83 . Several W-containing peptides were shown to be noncompetitive, linear mixed-or parabolic mixed-type inhibitors of DPP-IV 83,94,116,119 . This suggests that these peptides do not directly bind to the active site of DPP-IV 94,120 .…”

Section: Peptidesmentioning

confidence: 99%

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Milk proteins as a source of tryptophan-containing bioactive peptides

Nongonierma

Fitzgerald

2015

Food Funct.

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Tryptophan (W) is an essential amino acid which is primarily required for protein synthesis. It also acts as 5 a precursor of key biomolecules for human health (serotonin, melatonin, tryptamine, niacin, nicotinamide adenine dinucleotide (NAD), phosphorylated NAD (NADP), quinolinic acid, kynureric acid, etc.). Among dietary proteins, milk proteins are particularly rich in W. W residues within milk proteins may be released by proteolytic/peptidolytic enzymes either as a free amino acid or as part of peptide sequences. Different W-containing peptides originating from milk proteins have been shown in vitro to display a 10 wide range of bioactivities such as angiotensin converting enzyme (ACE) inhibition along with antioxidant, antidiabetic and satiating related properties. Free W has been shown in certain instances to have an effect on cognition and the aforementioned bioactive properties. However, a higher bioactive potency has generally been observed with specific W-containing peptides compared to free W. Since W is thermolabile, the impact of processing on the stability of W-containing peptides needs to be considered. 15Milk protein-derived W-containing peptides may have significant potential as natural health promoting agents in humans.

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Section: Article Type Wwwrscorg/xxxxxx | Xxxxxxxxmentioning

confidence: 99%

Section: Peptidesmentioning

confidence: 99%

Milk proteins as a source of tryptophan-containing bioactive peptides

Nongonierma

Fitzgerald

2015

Food Funct.

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“…Previously published DPP-IV IC 50 values for the amino acids which were found within the NF permeate are shown in Table 3 (Nongonierma, Mooney, Shields, & FitzGerald, 2013). In addition, IW, LW, WL, WI VA, GL, FW, WF and VL have also been previously evaluated for their DPP-IV inhibitory potential (Lan, Ito, Ito, & Kawarasaki, 2014;Lan et al, 2015;Nongonierma & FitzGerald, 2013a, 2013dTulipano et al, 2011). Three peptides reported for the first time (CIVL, LCVL and GI) were evaluated for their in vitro DPP-IV inhibitory properties in this study (Table 2).…”

Section: Confirmatory Study Of Dpp-iv Inhibitory Activity With Synthementioning

confidence: 99%

Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate

Maux

Nongonierma

Murray

et al. 2015

Food Research International

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“…Five previously identified DPP-IV inhibitory dipeptides (GY, GL, GI, NY and WL) were predicted to be released following in silico digestion of -La by elastase (Table 1). Of the peptides predicted to be released by elastase, WL is a relatively potent DPP-IV inhibitory peptide with an IC 50 of 43.6 µM 16 . Overall, of the enzymes studied, elastase was predicted to release the highest number of previously identified DPP-IV inhibitory peptides or peptides with DPP-IV inhibitory motifs (with a W at the N-terminus).…”

Section: In Silico Digestion Of -Lamentioning

confidence: 99%

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

et al. 2016

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Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibitory peptide sequences. An α-La isolate was hydrolysed with elastase under different conditions using an experimental design approach incorporating 3 factors (temperature, pH and enzyme to substrate ratio (E:S) ratio) at 2 levels. The hydrolyzate generated at pH 8.5, 50C, E:S 2.0% (w/w) (H9) displayed the lowest half maximal DPP-IV inhibitory concentration (IC50 = 1.20 ± 0.12 mg mL -1). Five α-La-derived DPP-IV inhibitory peptides (GY, GL, GI, NY and WL) predicted to be released in silico were identified by liquid-chromatography tandem mass spectrometry (LC-MS/MS) within H9 and its simulated gastrointestinal digestion (SGID) sample. This proof of concept study demonstrated the benefit of using a targeted approach combined with an experimental design in the generation of dietary protein hydrolyzates with DPP-IV inhibitory properties. IntroductionDipeptidyl peptidase IV (DPP-IV) is an ubiquitous enzyme which is responsible for the cleavage and inactivation of the incretin hormones, glucose dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) 1 . In the context of type 2 diabetes management, DPP-IV inhibition may be used as a means to improve the regulation of serum glucose in humans. Various DPP-IV inhibitory drugs (gliptins), have been developed to maintain the insulinotropic activity of the incretins in the post-prandial phase 2 .Dietary components, including food protein-derived peptides, have been shown to play a role in the inhibition of DPP-IV in vitro and in certain instances in vivo, for reviews, see: 3,4,5 . In silico studies have shown that selected DPP-IV inhibitory peptide sequences may be found within a wide range of dietary proteins 6,7 . To date, milk proteins appear to be the most frequently studied substrate for the generation of DPP-IV inhibitory peptides. Depending on the enzymatic strategy employed, different milk proteins may appear to be more suitable substrates for the production of DPP-IV inhibitory peptides. For instance, it was recently predicted by Tulipano et al.8 using in silico digestion with gastrointestinal proteinases that -lactoglobulin (-Lg) should yield a higher number of previously identified DPP-IV inhibitory peptides than -La. This was further confirmed following in vitro digestion of -Lg and -La with gastrointestinal enzymes, yielding hydrolyzates with IC 50 values of 0.74 and 1.70 mg mL -1, respectively 8 . Other in silico analysis of the major milk proteins indicated that -lactalbumin (-La) displayed the highest level of sequence coverage (43.9%) for previously identified DPP-IV inhibitory peptides as well as the highest DPP-IV inhibitory potency index (i.e., 17.9 10 -6 µM -1 g -1 ) 7 . It has been suggested that discrepancies between studies to determine the most adequate substrate for the genera...

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Inhibition of dipeptidyl peptidase IV (DPP-IV) by tryptophan containing dipeptides

Cited by 74 publications

References 36 publications

Milk proteins as a source of tryptophan-containing bioactive peptides

Milk proteins as a source of tryptophan-containing bioactive peptides

Identification of short peptide sequences in the nanofiltration permeate of a bioactive whey protein hydrolysate

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

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