21929-69-1

Basic information

• Product Name: Z-ALA-GLY-GLY-OH
• Synonyms: Z-L-ALANYLGLYCYLGLYCINE;Z-ALA-GLY-GLY-OH;N-CBZ-ALA-GLY-GLY
• CAS NO: 21929-69-1
• Molecular Formula: C₁₅H₁₉N₃O₆
• Molecular Weight: 337.33
• Mol File: 21929-69-1.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-ALA-GLY-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-ALA-GLY-GLY-OH(21929-69-1)
• EPA Substance Registry System: Z-ALA-GLY-GLY-OH(21929-69-1)

Safety Data

• Hazardous Substances Data: 21929-69-1(Hazardous Substances Data)

Usage

General Description

Z-ALA-GLY-GLY-OH is a peptide composed of three amino acids: alanine (ALA), glycine (GLY), and glycine (GLY). The Z- prefix indicates that the amino end of the molecule has been modified with a protecting group to prevent unwanted reactions during peptide synthesis. This peptide is often used in biochemical and medical research as a building block for creating larger peptides and proteins. It can also be used as a substrate for studying the enzymatic activity of proteases and peptidases. Additionally, Z-ALA-GLY-GLY-OH may have potential therapeutic applications in drug development due to its ability to interact with biological systems and potentially affect cellular processes.

Upstream product

• 501-53-1 benzyl chloroformate 
• 2503-31-3 N-benzyloxycarbonyl-L-alanylglycine 
• 4840-29-3 Z-L-Ala-Gly-OMe 
• 1142-20-7 N-Cbz-Ala 
• 556-50-3 glycylglycine 
• 25516-39-6 pentafluorophenyl ester of benzyloxycarbonylalanine 

Downstream Products

• 136206-20-7 17β-(N-benzyloxycarbonyl-L-alanyl-glycyl-glycyl)aminoestra-1,3,5(10)-trien-3-ol 
• 3146-40-5 L-alanylglycylglycine 
• 125816-03-7 [2-((S)-2-Benzyloxycarbonylamino-propionylamino)-acetylamino]-acetic acid 2-cyano-ethyl ester 

Relevant articles and documents

Engineered Substrate for Cyclooxygenase-2: A Pentapeptide Isoconformational to Arachidonic Acid for Managing Inflammation

Beyond the conventional mode of working of anti-inflammatory agents through enzyme inhibition, herein, COX-2 was provided with an alternate substrate. A proline-centered pentapeptide isoconformational to arachidonic acid, which exhibited appreciable selectivity for COX-2, overcoming acetic acid- and formalin-induced pain in rats to almost 80%, was treated as a substrate by the enzyme. Remarkably, COX-2 metabolized the pentapeptide into small fragments consisting mainly of di- and tripeptides that ensured the safe breakdown of the peptide under in vivo conditions. The kinetic parameter Kcat/Km for COX-2-mediated metabolism of the peptide (6.3 × 105 M-1 s-1) was quite similar to 9.5 × 105 M-1 s-1 for arachidonic acid. Evidenced by the molecular dynamic studies and the use of Y385F COX-2, it was observed that the breakage of the pentapeptide has probably been taken place through H-bond activation of the peptide bond by the side chains of Y385 and S530.