140945-51-3

Usage

Uses

Used in Pharmaceutical Industry:
N-ACETYL-L-GLYCYL-L-GLUTAMINE is used as a therapeutic agent for gastrointestinal disorders, liver disease, and muscle wasting due to its antioxidant and anti-inflammatory properties.
Used in Sports Nutrition Industry:
N-ACETYL-L-GLYCYL-L-GLUTAMINE is used as a dietary supplement to support athletic performance and recovery, potentially enhancing muscle growth and reducing muscle fatigue.
Used in Research and Development:
N-ACETYL-L-GLYCYL-L-GLUTAMINE is used as a subject of ongoing research to explore its potential applications in various fields, including medicine, nutrition, and sports performance.

Upstream product

• 56-85-9 L-glutamine 

Relevant academic research and scientific papers

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.

N-acyl dipeptides and their compositions

Novel a-acyl dipeptides of the formula: in which AS, R1 and R2 have certain, more precisely defined meanings. These N-acyl dipeptides are more stable under conditions of sterilization (121° C.) than corresponding, non-acylated dipept