17664-94-7

Basic information

• Product Name: N-CARBOBENZOXY-L-LEUCYL-L-ALANINE BENZYL ESTER
• Synonyms: N-CBZ-L-LEUCYL-L-ALANINE BENZYL ESTER;N-CARBOBENZOXY-L-LEUCYL-L-ALANINE BENZYL ESTER;Carbobenzoxyleucylalaninebenzylester;N-(N-Carbobenzoxy-L-leucyl)-L-alanine benzyl ester;N-(N-Cbz-L-leucyl)-L-alanine benzyl ester;N-Benzyloxycarbonyl-L-Leu-L-Ala-OBzl;N-Cbz-L-Leu-L-Ala-OBzl
• CAS NO: 17664-94-7
• Molecular Formula: C₂₄H₃₀N₂O₅
• Molecular Weight: 426.51
• Mol File: 17664-94-7.mol
• Article Data: 3

Chemical Properties

• Appearance: /
• CAS DataBase Reference: N-CARBOBENZOXY-L-LEUCYL-L-ALANINE BENZYL ESTER(CAS DataBase Reference)
• NIST Chemistry Reference: N-CARBOBENZOXY-L-LEUCYL-L-ALANINE BENZYL ESTER(17664-94-7)
• EPA Substance Registry System: N-CARBOBENZOXY-L-LEUCYL-L-ALANINE BENZYL ESTER(17664-94-7)

Safety Data

• Hazardous Substances Data: 17664-94-7(Hazardous Substances Data)

Upstream product

• 2018-66-8 Z-Leu-OH 
• 5557-81-3 L-alanine benzyl ester hydrochloride 
• 42854-62-6 L-alanine benzyl ester p-toluenesulfonate 
• 53363-87-4 N-(benzyloxycarbonyl)leucine dicyclohexylamine salt 

Downstream Products

• 7298-84-2 Leu-Ala 
• 75779-22-5 H-Leu-Ala-OH 

Relevant articles and documents

Recyclable hypervalent iodine(III) reagent iodosodilactone as an efficient coupling reagent for direct esterification, amidation, and peptide coupling

A hypervalent iodine(III) reagent plays a novel role as an efficient coupling reagent to promote the direct condensation between carboxylic acids and alcohols or amines to provide esters, macrocyclic lactones, amides, as well as peptides without racemization. The regeneration of iodosodilactone (1) can also be readily achieved. The intermediate acyloxyphosphonium ion C from the activation of a carboxylic acid is thought to be involved in the present esterification reaction.

Role of basic and acidic fragments in delicious peptides (Lys-Gly-Asp-Glu-Glu-Ser-Leu-Ala) and the taste behavior of sodium and potassium salts in acidic oligopeptides.

The role of the acidic fragment (Asp-Glu-Glu) in delicious peptides was investigated in detail by using the Na+ or K+ salts of acidic oligopeptides so that amount of Na+ or K+ intake of peptides composed of acidic amino acids could be varied by changing their sequences. The taste of these peptides was confirmed to vary with Na+ or K+ intake. Additionally, in order to study the role of basic (Lys-Gly) and acidic (Asp-Glu-Glu) fragments in delicious peptides for producing the taste, five delicious peptide analogs, Ser-Leu-Ala-Lys-Gly-Asp-Glu-Glu, Ser-Leu-Ala-Asp-Glu-Glu-Lys-Gly, Lys-Gly-Ser-Leu-Ala-Asp-Glu-Glu, Lys-Gly-Asp-Glu-Glu, and Glu-Glu-Asp-Gly-Lys, were synthesized. The intensity of the umami and/or salty taste of these peptides and their Na salts was almost the same, despite their chemical structures being different. These results indicate that the acidic fragment as well as the basic fragment plays an important role in the taste production and intensity of delicious peptides, and that an umami or salty taste can be produced by the localization of the cation of the basic fragment and the anion of the acidic fragment.