3790-51-0

Usage

Definition

ChEBI: A dipeptide composed of L-aspartic acid and glycine joined by a peptide linkage.

InChI:InChI=1/C6H10N2O5/c7-3(1-4(9)10)6(13)8-2-5(11)12/h3H,1-2,7H2,(H,8,13)(H,9,10)(H,11,12)

Upstream product

• 142757-75-3 isoasparaginylglycine 
• 64817-62-5 t-butoxycarbonyl-L-asparagine anhydride 
• 39552-95-9 N-(N-benzyloxycarbonyl-L-α-aspartyl)-glycine ethyl ester 
• 503027-29-0 N-Benzyl-α-L-aspartyl-glycin-aethylester 
• 55247-97-7 (S)-N-[Bis-(4-methoxy-phenyl)-methyl]-2-tert-butoxycarbonylamino-succinamic acid 
• 3338-32-7 Z-Asp(OtBu)-OSu 
• 56-40-6 glycine 
• 93566-85-9 N-Benzyl-α-L-aspartyl-glycin 
• 40470-02-8 N-(O-benzyl-N-benzyloxycarbonyl-L-α-aspartyl)-glycine benzyl ester 

Relevant academic research and scientific papers

PEPTIDE COMPOUNDS AND METHODS OF USING PEPTIDE COMPOUNDS TO TREAT CONDITIONS AFFECTING THE CARDIAC, PULMONARY, AND NERVOUS SYSTEMS

The present invention provides a method of treating or preventing diseases or conditions affecting the cardiac, pulmonary and/or nervous systems in a subject using peptide compounds. The methods of the invention are useful for the treatment and prevention of a variety of disorders or conditions including, without limitation, ischemia, stroke, pulmonary diseases, allergic reactions, physical trauma to pulmonary tissues, exposure to harmful entities in the environment, and smoking.

Rates of reduction of N-chlorinated peptides by sulfite: Relevance to incomplete dechlorination of wastewaters

Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N- chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N- chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and / ? 0.1 M is as follows: rate = (9.92 ± 0.41 x 103[H2PO4-] + 5.70 ± 0.52 x 108[H3O+] + 5.3 ± 0.2)[SO32-][Cl- Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable S(IV) doses and pH values. Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N-chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N-chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and I≈0.1 M is as follows: rate = (9.92±0.41×103[H2 PO4- ]+5.70±0.52×108[ H3O+]+5.3±0.2) [SO32-][Cl-Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable SIV doses and pH values.

A Quantitative Evaluation of Methods for Coupling Asparagine

A quantitative procedure was developed to evaluate methods for coupling asparagine.Boc-asparagine was coupled to glycyloxymethylphenoxymethyl-copoly(styrene-divinylbenzene) resin under a variety of conditions, and the product, Asn-Gly, and any byproducts were cleaved from the resin with 50percent trifluoroacetic acid in methylene chloride.The mixture was then separated on a sulfonated ion exchange column and quantitated by the ninhydrin reaction.Coupling by the dicyclohexylcarbodiimide (DCC) or symmetrical anhydride methods gave large amounts of the dehydration product, β-cyanoalanylglycine, and smaller amounts of β-aspartamidinoacetic acid, α-aspartylglycine, and β-aspartylglycine in addition to the desired asparaginylglycine.Activation of Boc-Asn by DCC plus hydroxybenzotriazole or by the nitrophenyl ester gave 98 to 99percent of Asn-Gly, but very low levels of the byproducts were detectable with the sensitive chromatographic method.Protection of the amide function of Boc-Asn with the 4,4'-dimethoxybenzhydryl group avoided completely the formation of the nitrile during DCC coupling.Pure Ala(CN)-Gly was quantitatively reconverted to Asn-Gly by HF.The rehydration of nitrile also occurred in 50percent trifluoroacetic acid in dichloromethane, but much more slowly.

Isolation and identification of urinary β-aspartyl dipeptides and their concentrations in human urine

β-Aspartyl-methionine, -aspartic acid and -glutamic acid and γ-glutamyl-threonine and -glycine were isolated and identified in human urine by means of ion-exchange chromatography, highvoltage paper electrophoresis, acid hydrolysis and determination of N-terminal amino acids of the isolated compounds, and comparison of their behaviors in paper electrophoresis and chromatography with those of the authentic compounds. The concentrations of acidic β-aspartyl dipeptides in human urine were determined using an amino acid analyzer. Their concentrations were as follows: β-aspartyl-glycine, male, 44.4±8.5, female, 61.4±18.9, child, 83.7±27.1; -alanine, male, 11.0±4.9, female, 20.7±12.0, child, 25.3±9.1; -glutamic acid, male, 10.0±3.7, female, 23.0±8.5, child, 20.4±7.5; -serine, male, 9.9±2.8, female, 13.6±3.8, child, 14.9±4.7; -aspartic acid, male, 4.3±1.0, female, 9.1±2.2, child, 18.4±6.5; -threonine, male, 3.9±0.9, female, 5.8±1.1, child, 13.2±4.9 μmol/g creatinine (mean ± S.D.). The order of the sum of their concentrations tended to be child>female>male. Patients receiving intravenous hyperalimentation also excreted acidic β-aspartyl dipeptides into urine in amounts similar to those in females and in a pattern similar to that observed in healthy persons. This finding indicates that urinary β-aspartyl dipeptides were probably of endogenous origin because oral nutrition was stringently excluded in these patients.