Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme

Lunow, Diana; Kaiser, Susanne; Rückriemen, Jana; Pohl, Christoph; Henle, Thomas

doi:10.1016/j.foodchem.2014.06.059

Cited by 36 publications

(30 citation statements)

References 33 publications

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“…It should be noted that the tryptophan-containing dipeptides, including IleTrp and LeuTrp, which have been found in food protein hydrolysates, are inhibitors of angiotensin converting enzyme (ACE) involved in the regulation of blood pressure [24]. The peptide IleTrp is a selective and competitive inhibitor of the C-terminal domain of the enzyme possessing a selectivity coefficient of 40 compared to the N-terminal domain [24].…”

Section: Discussionmentioning

confidence: 99%

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

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Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity.

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Section: Discussionmentioning

confidence: 99%

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Tran

Hoang

Nguyen

et al. 2017

Toxins

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“…These analyses indicated that the presence of branched chain amino acids (L and I) or C and G at the Nterminus and R, W, P, K, F or Y at the C terminus are associated with potent ACE inhibitory activity 24,27,30,59 . -CN (f163-164)), IW (α-La (f 59-60) and LF (f 267-268)) and VW (LF (f 346-347) and 50 LF (f 548-549)) were shown to be competitive inhibitors of human ACE 62,63 . The -La-derived peptides, IW and WL (α-La (f 104-105) and α-La (f 118-119)) were identified in milk proteinbased infant formulae 64 and in a whey protein hydrolysate generated with a combination of chymotrypsin and thermolysin 55 62 .…”

Section: Release Of Free W and W-containing Peptides During The Digesmentioning

confidence: 98%

“…Localisation of the W residue at the C-terminal position of dipeptides (RW and VW) has been correlated with higher ACE 65 inhibitory properties as compared to the reverse peptides (WR and WV). These differences were explained by the fact that higher hydrophobic interactions at the S2' hydrophobic sub-site of the C-domain of the ACE active site could take place when W was located at the C-terminal side of dipeptides 63 .…”

Section: Release Of Free W and W-containing Peptides During The Digesmentioning

confidence: 99%

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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“…Recently, we have shown that bioactive peptides with a C-terminal tryptophan moiety and an Nterminal aliphatic amino acid (i.e. Ile-Trp or Ala-Trp) inhibit predominantly one active site, the C-domain, of ACE [13,14]. Thus, side effects of common hypotensive drugs like Captopril caused by unselective inhibition of both ACE-domains can be avoided [15].…”

Section: Introductionmentioning

confidence: 99%

Towards a continuous adsorption process for the enrichment of ACE-inhibiting peptides from food protein hydrolysates

Hippauf

Huettner

Lunow

et al. 2016

Carbon

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Tryptophan-containing dipeptides are C-domain selective inhibitors of angiotensin converting enzyme

Cited by 36 publications

References 33 publications

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Milk proteins as a source of tryptophan-containing bioactive peptides

Towards a continuous adsorption process for the enrichment of ACE-inhibiting peptides from food protein hydrolysates

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