Gluten Exorphin C
目录号 : GC30328GlutenexorphinC是一种源自谷朊粉的阿片肽。在GPI和MVD检测中,抑制μopioid和δopioid活性,IC50值分别为40μM和13.5μM。
Cas No.:142479-62-7
Sample solution is provided at 25 µL, 10mM.
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Gluten exorphin C is an opioid peptide derived from wheat gluten. Its IC50 values are 40 μM and 13.5 μM for μ opioid and δ opioid activities in the GPI and MVD assays, respectively.
Gluten exorphin C, a novel opioid peptide, is isolated from the pepsin-trypsin-chymotrypsin digest of wheat gluten. Gluten exorphin C is evaluated its opioid activities by the GPI and MVD assays and its receptor affinities by radioreceptor assays. Its IC50s are 40 μM and 13.5 μM in the GPI and the MVD assays, respectively. Gluten exorphin C has a structure quite different from any of the endogenous and exogenous opioid peptides ever reported in that the N terminal Tyr is the only aromatic amino acid. The analogs containing Tyr-Pro-X-Ser-Leu are synthesized to study its structure-activity relationship. Peptides in which X is an aromatic amino acid or an aliphatic hydrophobic amino acid has opioid activity[1].
[1]. Fukudome S, et al. Gluten exorphin C. A novel opioid peptide derived from wheat gluten. FEBS Lett. 1993 Jan 18;316(1):17-9.
Cas No. | 142479-62-7 | SDF | |
Canonical SMILES | Tyr-Pro-Ile-Ser-Leu | ||
分子式 | C29H45N5O8 | 分子量 | 591.7 |
溶解度 | Soluble in DMSO | 储存条件 | Store at -20°C |
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1 mg | 5 mg | 10 mg | |
1 mM | 1.69 mL | 8.4502 mL | 16.9005 mL |
5 mM | 0.338 mL | 1.69 mL | 3.3801 mL |
10 mM | 0.169 mL | 0.845 mL | 1.69 mL |
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Gluten exorphin C. A novel opioid peptide derived from wheat gluten
A novel opioid peptide, Tyr-Pro-Ile-Ser-Leu, was isolated from the pepsin-trypsin-chymotrypsin digest of wheat gluten. Its IC50 values were 40 microM and 13.5 microM in the GPI and MVD assays, respectively. This peptide was named gluten exorphin C. Gluten exorphin C had a structure quite different from any of the endogenous and exogenous opioid peptides ever reported in that the N terminal Tyr was the only aromatic amino acid. The analogs containing Tyr-Pro-X-Ser-Leu were synthesized to study its structure-activity relationship. Peptides in which X was an aromatic amino acid or an aliphatic hydrophobic amino acid had opioid activity.
Genetic predictors of celiac disease, lactose intolerance, and vitamin D function and presence of peptide morphins in urine of children with neurodevelopmental disorders
Gastrointestinal disturbances, nutritional deficiencies, and food intolerances are frequently observed in children with neurodevelopmental disorders (NDD). To reveal possible association of celiac disease risk variants (HLA-DQ), lactose intolerance associated variant (LCT-13910C>T) as well as variant associated with vitamin D function (VDR FokI) with NDD, polymerase chain reaction-based methodology was used. Additionally, intestinal peptide permeability was estimated in NDD patients and healthy children by measuring the level of peptides in urine using high-performance liquid chromatography. Levels of opioid peptides, casomorphin 8, and gluten exorphin C were significantly elevated in urine samples of NDD patients (P = 0.004 and P = 0.005, respectively), but no association of genetic risk variants for celiac disease and lactose intolerance with NDD was found. Our results indicate that increased intestinal peptide permeability observed in analyzed NDD patients is not associated with genetic predictors of celiac disease or lactose intolerance. We have also found that FF genotype of VDR FokI and lower serum levels of vitamin D (25-OH) showed association with childhood autism (CHA), a subgroup of NDD. We hypothesize that vitamin D might be important for the development of CHA.
Opioid peptides derived from food proteins suppress aggregation and promote reactivation of partly unfolded stressed proteins
A new view of the opioid peptides is presented. The potential of small peptides derived from precursor food proteins, to bind to partly unfolded stressed proteins to prevent their irreversible aggregation and inactivation has been demonstrated in various in vitro test systems: dithiothreitol-induced aggregation of alpha-lactalbumin (LA), heat-induced aggregation of alcohol dehydrogenase (ADH), and aggregation and inactivation of bovine erythrocyte carbonic anhydrase (CA) in the process of its refolding after removal of stress conditions. Using dynamic light scattering (DLS), turbidimetry, fluorescence, and circular dichroism measurements protective effects of the synthetic opioid peptides: exorphin C from wheat gluten (Tyr-Pro-Ile-Ser-Leu), rubiscolin-5 from spinach ribulose-bisphosphate-carboxylase/oxygenase (Rubisco) (Tyr-Pro-Leu-Asp-Leu), and hemorphin-6 from bovine hemoglobin (Tyr-Pro-Trp-Thr-Gln-Arg) have been revealed. We have demonstrated the concentration-dependent suppression of light scattering intensity of aggregates of LA and ADH in the presence of the peptides, the population of nanoparticles with higher hydrodynamic radii being shifted to the lower ones, accompanied by an increase in the lag period of aggregation. The presence of the peptides in the refolding solution was shown to assist reactivation of CA and enhance the yield of the CA soluble protein. The results suggest that bioactive food protein fragments may be regarded as exogenous supplements to the endogenous defense mechanisms of the human organism under stress conditions.