140945-51-3

Basic information

• Product Name: N-ACETYL-L-GLYCYL-L-GLUTAMINE
• Synonyms: N-ACETYL-L-GLYCYL-L-GLUTAMINE;N-Acetyl-Glycyl-L-Glutamine;(S)-2-(2-AcetaMidoacetaMido)-5-aMino-5-oxopentanoic acid
• CAS NO: 140945-51-3
• Molecular Formula: C9H15N3O5
• Molecular Weight: 245.23
• Mol File: 140945-51-3.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• CAS DataBase Reference: N-ACETYL-L-GLYCYL-L-GLUTAMINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-ACETYL-L-GLYCYL-L-GLUTAMINE(140945-51-3)
• EPA Substance Registry System: N-ACETYL-L-GLYCYL-L-GLUTAMINE(140945-51-3)

Safety Data

• Hazardous Substances Data: 140945-51-3(Hazardous Substances Data)

Usage

General Description

N-acetyl-L-glycyl-L-glutamine, also known as NAGG, is a dipeptide composed of L-glycine and L-glutamine linked together by an amide bond. It is a naturally occurring compound found in the body and is involved in various biological processes. NAGG has been shown to have antioxidant and anti-inflammatory properties, and has been studied for its potential therapeutic effects in conditions such as gastrointestinal disorders, liver disease, and muscle wasting. It has also been explored for its potential use as a dietary supplement to support athletic performance and recovery. Overall, N-acetyl-L-glycyl-L-glutamine is a compound with diverse potential applications and is the subject of ongoing research.

Upstream product

• 56-85-9 L-glutamine 

Relevant articles and documents

Peptide ligation by chemoselective aminonitrile coupling in water

Amide bond formation is one of the most important reactions in both chemistry and biology1–4, but there is currently no chemical method of achieving α-peptide ligation in water that tolerates all of the 20 proteinogenic amino acids at the peptide ligation site. The universal genetic code establishes that the biological role of peptides predates life’s last universal common ancestor and that peptides played an essential part in the origins of life5–9. The essential role of sulfur in the citric acid cycle, non-ribosomal peptide synthesis and polyketide biosynthesis point towards thioester-dependent peptide ligations preceding RNA-dependent protein synthesis during the evolution of life5,9–13. However, a robust mechanism for aminoacyl thioester formation has not been demonstrated13. Here we report a chemoselective, high-yielding α-aminonitrile ligation that exploits only prebiotically plausible molecules—hydrogen sulfide, thioacetate12,14 and ferricyanide12,14–17 or cyanoacetylene8,14—to yield α-peptides in water. The ligation is extremely selective for α-aminonitrile coupling and tolerates all of the 20 proteinogenic amino acid residues. Two essential features enable peptide ligation in water: the reactivity and pKaH of α-aminonitriles makes them compatible with ligation at neutral pH and N-acylation stabilizes the peptide product and activates the peptide precursor to (biomimetic) N-to-C peptide ligation. Our model unites prebiotic aminonitrile synthesis and biological α-peptides, suggesting that short N-acyl peptide nitriles were plausible substrates during early evolution.