27440-00-2

Upstream product

• 3757-98-0 Ac-Gly-Gly-OEt 
• 16438-42-9 glycylglycine amide hydrochloride 
• 108-24-7 acetic anhydride 
• 1668-10-6 glycinamide hydrochloride 
• 543-24-8 N-acetylglycine 
• 598-41-4 H-Gly-NH₂ 

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.

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 pepti

The partial molar volume and heat capacity of the glycyl group in aqueous solution at 25°C

The partial molar volumes, V°2, and the partial molar heat capacities, C°p,2, at infinite dilution have been determined for three new peptides of sequence seryl(glycyl)xglycine, where x=0 to 2, in aqueous solution at 25°C.

Anticonvulsant drugs and pharmaceutical compositions thereof

According to the present invention, anticonvulsant compounds N-acetyl,N'-benzylglycinamide and N-benzyloxycarbonylglycinamide-Z-glycinamide are disclosed. The present invention also discloses an anticonvulsant pharmaceutical composition comprising an effe

Aqueous Solutions Containing Amino Acids and Peptides

The energetics of the interactions occuring between some N-acetyl amino acid amides and some N-acetyl peptide amides in aqueous solutions at 298.15 K have been investigated.Osmotic coefficients of solutions containing N-acetylglycinamide (G), N-acetyl-L-a