6157-06-8

Usage

Definition

ChEBI: A dipeptide formed from L-alpha-aspartyl and L-glutamic acid residues.

InChI:InChI=1/C9H14N2O7/c10-4(3-7(14)15)8(16)11-5(9(17)18)1-2-6(12)13/h4-5H,1-3,10H2,(H,11,16)(H,12,13)(H,14,15)(H,17,18)/t4-,5-/m0/s1

Upstream product

• 112842-55-4 N-(N-benzyloxycarbonyl-L-α-aspartyl)-L-glutamic acid diethyl ester 
• 16450-41-2 L-glutamic acid diethyl ester 
• 56-84-8 L-Aspartic acid 
• 56-86-0 L-glutamic acid 
• 104870-27-1 N-(O-benzyl-N-benzyloxycarbonyl-L-α-aspartyl)-L-glutamic acid dibenzyl ester 
• 73618-80-1 N-(N-benzyloxycarbonyl-L-α-aspartyl)-L-glutamic acid 

Downstream Products

• 56-84-8 L-Aspartic acid 
• 56-86-0 L-glutamic acid 

Relevant academic research and scientific papers

Green fluorescent protein fusions with random peptides

The invention relates to the use of fluorescent proteins, particularly green fluorescent protein (GFP), in fusion constructs with random and defined peptides and peptide libraries, to increase the cellular expression levels, decrease the cellular catabolism, increase the conformational stability relative to linear peptides, and to increase the steady state concentrations of the random peptides and random peptide library members expressed in cells for the purpose of detecting the presence of the peptides and screening random peptide libraries. N-terminal, C-terminal, dual N- and C-terminal and one or more internal fusions are all contemplated. Novel fusions utilizing self-binding peptides to create a conformationally stabilized fusion domain are also contemplated.

The Relationship between Taste and Primary Structure of "Delicious Peptide" (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) from Beef Soup

"Delicious peptide" was reported to be as delicious as beef soup.The peptide and its fragments were synthesized to study its taste active sites. "Delicious peptide" was found to produce a umami and a sour taste.By preparing several di- or tripeptides composed of basic or acidic amino acids, we found that the taste of "delicious peptide" was produced by an interaction between the basic and the acidic fragments in the peptide.

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.