14485-80-4

Basic information

• Product Name: Z-PRO-LEU-GLY-NH2
• Synonyms: N-CBZ-PRO-LEU-GLY AMIDE;Z-L-PROLYL-L-LEUCYL-GLYCYL AMIDE;Z-PRO-LEU-GLY-NH2;z-pro-leu-gly amide;carbobenzoxyprolyl-leucyl-glycinamide;N-carbobenzyloxy-Pro-Leu-Gly amide;(2S)-2-[[(1S)-1-[(2-amino-2-keto-ethyl)carbamoyl]-3-methyl-bu;(2S)-2-[[[(1S)-1-[[(2-amino-2-oxoethyl)amino]-oxomethyl]-3-methylbutyl]amino]-oxomethyl]-1-pyrrolidinecarboxylic acid phenylmethyl ester
• CAS NO: 14485-80-4
• Molecular Formula: C₂₁H₃₀N₄O₅
• Molecular Weight: 418.49
• Product Categories: Dipeptides and Tripeptides;Peptides;Tripeptides
• Mol File: 14485-80-4.mol
• Article Data: 7

Chemical Properties

• Boiling Point: 731 °C at 760 mmHg
• Flash Point: 395.9 °C
• Appearance: /
• Density: 1.195 g/cm³
• Vapor Pressure: 3.14E-21mmHg at 25°C
• Refractive Index: 1.556
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-PRO-LEU-GLY-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PRO-LEU-GLY-NH2(14485-80-4)
• EPA Substance Registry System: Z-PRO-LEU-GLY-NH2(14485-80-4)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 14485-80-4(Hazardous Substances Data)

Usage

General Description

Z-PRO-LEU-GLY-NH2 is a peptide comprised of the amino acids proline, leucine, and glycine connected in a specific sequence. The "Z" in the name refers to the protective group on the N-terminus, while "NH2" denotes the presence of an amino group at the C-terminus. This peptide is commonly used in research and pharmaceutical applications, such as in the study of protein structure and function, drug development, and as a potential therapeutic agent. It may also have potential applications in fields such as cosmetics and food additives due to its amino acid composition and potential biological activities. Overall, Z-PRO-LEU-GLY-NH2 has diverse potential uses and continues to be an area of active research and development.

InChI:InChI=1/C21H30N4O5/c1-14(2)11-16(19(27)23-12-18(22)26)24-20(28)17-9-6-10-25(17)21(29)30-13-15-7-4-3-5-8-15/h3-5,7-8,14,16-17H,6,9-13H2,1-2H3,(H2,22,26)(H,23,27)(H,24,28)

Upstream product

• 82636-86-0 L-Leucyl-glycine amide trifluoroacetate 
• 1148-11-4 N-Benzyloxycarbonyl-L-proline 
• 39705-58-3 L-Leucylglycinamide 
• 545390-97-4 (S)-2-(2-Carboxy-ethylsulfanylcarbonyl)-pyrrolidine-1-carboxylic acid benzyl ester 
• 1738-87-0 Z-Leu-ONp 
• 2018-66-8 Z-Leu-OH 
• 545390-93-0 Z-Pro-SMe 
• 119706-28-4 Z-Pro-Leu-Gly-OBg 
• 2873-37-2 -L-leucine methyl ester 
• 598-41-4 H-Gly-NH₂ 
• 55264-42-1 glycine amide hydrobromide 
• 7784-82-9 N-[N-(N-benzyloxycarbonyl-L-prolyl)-L-leucyl]glycine ethyl ester 
• 2867-06-3 Benzyloxycarbonylleucyl-glycine ethyl ester 
• 38173-66-9 HCl_.H-Leu-Gly-NH₂ 

Downstream Products

• 51220-77-0 Cbz-Pro-Leu-Gly-OCH₃ 
• 83472-41-7 N-(chloro-2-ethyl) N-nitrosocarbamoyl L-prolyl L-leucyl glycinamide 
• 83472-43-9 N-methyl N-nitrosocarbamoyl L-prolyl L-leucyl glycinamide 
• 2002-44-0 melanostatin 

Relevant articles and documents

SYNTHESIS OF THE AMIDE OF THE C-TERMINAL TETRAPEPTIDE OF THE SEQUENCE OF OXYTOCIN

The synthesis has been effected of the amide of the tetrapeptide forming the sequence 6-9 of oxytocin with the use of benzyl protection of the thiol function of cysteine by two main schemes 1+3 and 2+2.The advantageousness of performing the synthesis by the 2+2 scheme has been shown.The overall yield of tetrapeptide using the method of condensation with the formation of mixed anhydrides amounted to 51percent by the scheme proposed.

Enzymatic C-terminal amidation of amino acids and peptides

Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.

PEPTIDE SYNTHESIS CATALYZED BY NATIVE PROTEINASE K IN WATER-MISCIBLE ORGANIC SOLVENTS WITH LOW WATER CONTENT

Rection of Ac-Tyr-OEt with HBr.Gly-NH2, catalysed by free proteinase K in various water-miscible organic solvents in the presence of triethylamine and 5 mol percent of water, was studied.Some aliphatic alcohols and acetonitrile proved to be suitable solvents.The effect of water content (2 percent - 20 percent) on the synthesis of Ac-Tyr-Gly-NH2 was studied using acetonitrile as solvent.Lowering of the water content to 5 percent or 2 percent led to almost 100 percent yield of the desired dipeptide; higher water content accelerated the reaction reducing at the same time the yield of Ac-Tyr-Gly-NH2 due to the concurrent hydrolysis of the ester Ac-Tyr-OEt.No reaction was observed in the absence of base (triethylamine), wereas an excess of base only retarded the reaction.The enzyme is capable of catalyzing the peptide bond synthesis with N-acylamino acids or N-acyl peptides as acylating components, which may contain all types of L-amino acid residues (except Pro) in the P1 position.However, the peptide bond synthesis depends strongly on the amino component composition, particularly on the amino acid residue in the P'1 position.Only amides of glycine and of hydrophillic amino acids were acylated with Ac-Tyr-OEt; amides of hydrophobic amino acids enter the reaction only reluctantly or not at al.The presence of Leu or Phe in position P'2 and Leu in position P'3 has not so negative effect on acylation of the amino component as has in presence in the P'1 position.The choice of protecting groups for the α-carboxyl of the amino component is restricted only to amide and in some cases its undesired enzymatic removal was observed.Unprotected peptides seem to be suitable amino components.