75188-89-5

Basic information

• Product Name: H-PRO-LEU-GLY-GLY-OH
• Synonyms: H-PRO-LEU-GLY-GLY-OH;MIF-1-Gly
• CAS NO: 75188-89-5
• Molecular Formula: C₁₅H₂₆N₄O₅
• Molecular Weight: 285.34
• Mol File: 75188-89-5.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-PRO-LEU-GLY-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-PRO-LEU-GLY-GLY-OH(75188-89-5)
• EPA Substance Registry System: H-PRO-LEU-GLY-GLY-OH(75188-89-5)

Safety Data

• Hazardous Substances Data: 75188-89-5(Hazardous Substances Data)

Usage

General Description

H-PRO-LEU-GLY-GLY-OH is a sequence of amino acids that form a peptide chain. It consists of proline (PRO), leucine (LEU), glycine (GLY), and another glycine (GLY) at the C-terminal, indicated by the -OH. These amino acids are organic compounds that are essential building blocks of proteins and play various roles in biological processes. Proline is known for its structural properties and is often found in the turns of protein structures, while leucine is important for protein synthesis and muscle development. Glycine is the simplest amino acid and acts as a neurotransmitter, while also playing a role in the synthesis of various compounds in the body. The H- at the beginning of the sequence indicates a protective group that may be used during the synthesis of peptides. Overall, H-PRO-LEU-GLY-GLY-OH is a specific sequence of amino acids that can be used for research purposes or in the synthesis of custom peptides.

Downstream Products

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• 117760-62-0 D-prolyl-L-leucylglycylglycine 
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• 36238-67-2 (3R,8aS)-hexahydro-3-(2-methylpropyl)pyrrolo[1,2-a]pyrazine-1,4-dione 
• 2873-36-1 (3S,8aR)-3-isobutyl-hexahydropyrrolo[1,2-a]pyrazine-1,4-dione 
• 2873-36-1 cyclo(L-Pro-L-Leu) 
• 117760-70-0 N-benzyloxycarbonyl-L-prolyl-L-leucylglycylglycine anilide 
• 117760-69-7 L-prolyl-L-leucylglycylglycine anilide 
• 68385-22-8 N-benzyloxycarbonyl-L-prolyl-L-leucylglycylglycine 

Relevant articles and documents

Model studies of competing hydrolysis and epimerization of some tetrapeptides of interest in amino acid racemization studies in geochronology

The processes of epimerization of individual peptide units in proteins and the concurrent cleavage of peptide bonds are modelled by heating some tetrapeptide and tetrapeptide derivatives to 148.5 deg C in pH 6.8 phosphate buffer.An excess of D-proline was observed during the heating of L-propyl-L-leucylglycylglycine.The D/L ratio of proline attains a maximum value of 2.1 after 90 minutes.The excess D-proline is attributed to the formation of a 2.3:1 mixture of diketopiperazines cyclo-(D-propyl-L-leucyl) and cyclo-(L-prolyl-L-leucyl).These two species account for most of the leucine and proline in the final mixture after the tetrapeptide is no longer detectable.Only small amounts of prolylleucine can be detcected after 50 hours.It is suggested that the above tetrapeptide undergoes internal aminolysis.Leucine in the tetrapeptide glycyl-L-leucylglycylglycine racemizes three times faster than in L-propyl-L-leucylglycylglycine.This demonstrates that an amino acid residue in a peptide chain does have an effect upon the rate of epimerization of a neighbouring peptide residue.A discussion of the geochemical implications of the results is included.