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Usage

Uses

Used in Pharmaceutical Industry:
Z-MET-GLY-OH is used as a building block for the synthesis of pharmaceuticals, contributing to the development of new drugs and therapeutic agents. Its unique structure and properties enable the creation of biologically active molecules with potential applications in various medical fields.
Used in Agrochemical Industry:
Z-MET-GLY-OH is used as a component in the synthesis of agrochemicals, such as pesticides and herbicides. Its incorporation into these compounds can enhance their effectiveness and selectivity, leading to improved crop protection and reduced environmental impact.
Used in Materials Science Applications:
Z-MET-GLY-OH is used as a building block in the development of advanced materials with specific properties. Its unique structure allows for the creation of materials with tailored characteristics, such as improved mechanical strength, thermal stability, or biocompatibility, depending on the application.
Used in Peptide Synthesis:
Z-MET-GLY-OH is used as a key component in peptide synthesis, allowing for the assembly of complex peptide sequences. Its presence in the synthesis process ensures the formation of stable and well-defined peptide structures, which can be further utilized in various research and industrial applications.

InChI:InChI=1/C15H20N2O5S/c1-23-8-7-12(14(20)16-9-13(18)19)17-15(21)22-10-11-5-3-2-4-6-11/h2-6,12H,7-10H2,1H3,(H,16,20)(H,17,21)(H,18,19)

Upstream product

• 27482-82-2 N-benzyloxycarbonyl-L-methionylglycine ethyl ester 
• 56-40-6 glycine 
• 3561-51-1 benzyl (S)-(1-hydrazinyl-4-(methylthio)-1-oxobutan-2-yl)carbamate 
• 501-53-1 benzyl chloroformate 
• 19519-01-8 N-(benzyloxycarbonyl)-L-methionylglycine methyl ester 
• 1152-62-1 Cbz-Met-OH 
• 144889-36-1 Z-Met-Gly-O^tBu 

Downstream Products

• 14486-03-4 N-L-methionyl-glycine 

Relevant academic research and scientific papers

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.

A One-Pot Peptide Synthesis via Se-phenyl Carboselenoate in Mixed Aqueous/Organic Solvent System

A one pot synthesis of peptides with free C-terminal residues has been accomplished via the active Se-phenyl carboselenoate using diphenyl diselenide, tributylphosphine, and N-methylmorpholine N-oxide in an acetonitrile- water mixed solvent system.Free amino acids and peptides have been used as the amine component without pH adjustment.

Improved efficiency and selectivity in peptide synthesis: Use of triethylsilane as a carbocation scavenger in deprotection of t-butyl esters and t-butoxycarbonyl-protected sites

The use of triethylsilane as a carbocation scavenger in the presence of trifluoroacetic acid in dichloromethane leads to increased yields, decreased reaction times, simple work-up and improved selectivity for the deprotection of t-butyl ester and t-butoxycarbonyl sites in protected amino-acids and peptides in the presence of other acid-sensitive protecting groups such as the benzyloxycarbonyl, 9-fluorenylmethoxycarbonyl, O- and S-benzyl and t-butylthio groups.