13171-96-5

Basic information

• Product Name: Z-LEU-PHE-NH2
• Synonyms: Z-LEU-PHE-NH2
• CAS NO: 13171-96-5
• Molecular Formula: C₂₃H₂₉N₃O₄
• Molecular Weight: 411.49
• Mol File: 13171-96-5.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 686.4±55.0 °C(Predicted)
• Appearance: /
• Density: 1.170±0.06 g/cm3(Predicted)
• Storage Temp.: -15°C
• PKA: 11.14±0.46(Predicted)
• CAS DataBase Reference: Z-LEU-PHE-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-LEU-PHE-NH2(13171-96-5)
• EPA Substance Registry System: Z-LEU-PHE-NH2(13171-96-5)

Safety Data

• Hazardous Substances Data: 13171-96-5(Hazardous Substances Data)

Upstream product

• 10473-38-8 N-(benzyloxycarbonyl)-L-leucyl-L-phenylalanine methyl ester 
• 5241-58-7 L-Phenylalanine amide 
• 51021-87-5 N-benzyloxycarbonyl-L-leucine methyl ester 
• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 
• 2018-66-8 Z-Leu-OH 
• 6401-63-4 N-benzyloxycarbonyl-L-leucyl-L-phenylalanine 
• 3005-89-8 ethyl N-benzyloxycarbonyl-L-leucyl-L-phenylalaninate 

Downstream Products

• 10473-38-8 N-(benzyloxycarbonyl)-L-leucyl-L-phenylalanine methyl ester 
• 6401-63-4 N-benzyloxycarbonyl-L-leucyl-L-phenylalanine 

Relevant articles and documents

Mechanoenzymatic peptide and amide bond formation

Mechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative of the valuable dipeptide L-alanyl-l-glutamine.

Efficient chemo-enzymatic synthesis of endomorphin-1 using organic solvent stable proteases to green the synthesis of the peptide

Endomorphin-1 (Tyr-Pro-Trp-Phe-NH2, EM-1), an effective analgesic, was efficiently synthesized by a combination of enzymatic and chemical methods. Peptide Boc-Trp-Phe-NH2 was synthesized with a high yield of 97.1% by the solvent-stab

C-terminal peptide amidation catalyzed by orange flavedo peptide amidase

The reverse reaction of amide hydrolysis can be achieved with the peptide amidase derived from oranges [Eq(1); Z=benzyloxycarbonyl]. The C-terminal carboxy group of the peptide is directly converted into an amide group by condensation with an ammonium salt. The amidation of peptides is of major interest since the biological activity of proteohormones and peptides is strongly influenced by the presence of a C-terminal amide group.