29852-55-9

Basic information

• Product Name: AC-GLY-LEU-OH
• Synonyms: N-ACETYL-GLY-L-LEU;AC-GLY-LEU-OH;ACETYL-GLYCYLLEUCINE;ACETYL-L-GLYCYL LEUCINE
• CAS NO: 29852-55-9
• Molecular Formula: C₁₀H₁₈N₂O₄
• Molecular Weight: 230.26
• Product Categories: Amino Acid Derivatives
• Mol File: 29852-55-9.mol
• Article Data: 6

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: AC-GLY-LEU-OH(CAS DataBase Reference)
• NIST Chemistry Reference: AC-GLY-LEU-OH(29852-55-9)
• EPA Substance Registry System: AC-GLY-LEU-OH(29852-55-9)

Safety Data

• Hazardous Substances Data: 29852-55-9(Hazardous Substances Data)

Usage

Description

AC-GLY-LEU-OH is a chemical compound consisting of three amino acids: acetyl (AC), glycine (GLY), and leucine (LEU), along with a carboxy terminal group (OH). It is commonly used in peptide synthesis and serves as a component of the peptide chain. The acetyl group at the N-terminus protects the amino group during synthesis, while the carboxy terminal group allows for further chemical modifications. Glycine and leucine, both essential amino acids, are crucial for protein synthesis and various metabolic processes in the body. AC-GLY-LEU-OH is valuable for its role in peptide synthesis and its potential for manipulation in different chemical applications.

Uses

Used in Pharmaceutical Industry:
AC-GLY-LEU-OH is used as a building block for drug development, contributing to the creation of more complex peptide structures and potentially leading to the discovery of new therapeutic agents.
Used in Biochemical Research:
In biochemical research, AC-GLY-LEU-OH is utilized for studying protein synthesis and various metabolic processes, as well as understanding the roles of glycine and leucine in biological systems.
Used in Peptide Synthesis:
AC-GLY-LEU-OH is used as a key component in peptide synthesis, where the acetyl group at the N-terminus protects the amino group, and the carboxy terminal group allows for further chemical modifications, enabling the development of diverse peptide-based compounds.

Upstream product

• 463-51-4 Ketene 
• 869-19-2 Glycyl-L-leucine 
• 108-24-7 acetic anhydride 
• 79780-41-9 (E)-2-(2-Acetylamino-acetylamino)-4-methyl-pent-2-enoic acid 
• 59652-62-9 Ac-Gly-Leu-OMe 
• 2666-93-5 (S)-Leu-OMe 
• 61-90-5 L-leucine 

Downstream Products

• 481054-29-9 N-acetylglycyl-L-leucyl-3-chloro-L-alanyl-L-phenylalanyl-L-alanine tert-butyl ester 
• 481054-30-2 N-acetylglycyl-L-leucyl-3-chloro-L-alanyl-L-phenylalanyl-L-alanine 

Relevant articles and documents

Postsynthetic Modification of Phenylalanine Containing Peptides by C-H Functionalization

New methods for peptide modification are in high demand in drug discovery, chemical biology, and materials chemistry; methods that modify natural peptides are particularly attractive. A Pd-catalyzed, C-H functionalization protocol for the olefination of phenylalanine residues in peptides is reported, which is compatible with common amino acid protecting groups, and the scope of the styrene reaction partner is broad. Bidentate coordination of the peptide to the catalyst appears crucial for the success of the reaction.

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