17790-87-3

Usage

Uses

Used in Pharmaceutical Research:
Boc-L-leucine hydrazide is utilized as a building block in the synthesis of peptide-based drugs, contributing to the development of new therapeutic agents. Its role in protecting and modifying amino acid residues is crucial for the creation of stable and effective bioactive molecules.
Used in Chemical Biology:
In the field of chemical biology, Boc-L-leucine hydrazide serves as a valuable tool for the modification of amino acid residues, enabling researchers to explore the interactions and functions of proteins and peptides with greater precision.
Used in Organic Synthesis:
Boc-L-leucine hydrazide is employed as a reagent in the synthesis of various organic compounds, showcasing its versatility and importance in organic chemistry. Its application in this field aids in the creation of a broad spectrum of chemical products.
Used in Drug Discovery:
As a component in drug discovery processes, Boc-L-leucine hydrazide is instrumental in the design and synthesis of potential drug candidates, particularly those that involve peptide sequences or require specific amino acid modifications for enhanced activity or stability.

Upstream product

• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 59-88-1 phenylhydrazine hydrochloride 
• 100-63-0 phenylhydrazine 

Downstream Products

• 77162-15-3 H-Leu-NHNHPh*TFA 
• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 14723-87-6 L-leucine phenylhydrazide 
• 474316-93-3 Boc-Leu-Pro-NHNHPh 
• 226543-67-5 Boc-Leu-Thr-NHNHPh 
• 64205-66-9 (tert-butoxycarbonyl)-L-leucyl-L-proline 

Relevant academic research and scientific papers

Stereocontrolled Total Synthesis of Muraymycin D1 Having a Dual Mode of Action against Mycobacterium tuberculosis

A stereocontrolled first total synthesis of muraymycin D1 (1) has been achieved. The synthetic route is highly stereoselective, featuring (1) selective β-ribosylation of the C2-methylated amino ribose, (2) selective Strecker reaction, and (3) ring-opening

Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis

The enzymatic cleavage of amino acid phenylhydrazides with the enzyme tyrosinase (EC 1.14.18.1) offers a new, mild, and selective method for C-terminal deprotection of peptides. The advantages of the described methodology are the very mild oxidative removal of the protecting group at room temperature and pH 7, a high chemo- and regioselectivity, and the availability of the biocatalyst. Even in oxygen-saturated solution, the oxidation of sensitive methionine residues was not observed. These features make the methodology suitable for the synthesis of sensitive peptide conjugates. Mechanistic data suggest that the hydrolysis of the oxidized adducts proceeds by a free-radical mechanism.

PAPAIN-CATALYZED SYNTHESIS OF PHENYLHYDRAZIDES OF N-ACYLAMINO ACIDS

Phenylhydrazides of Nα-acyl derivatives of all coded amino acids, except proline, were prepared by papain (E.C. 3.4.22.2)-catalyzed synthesis.Comparison of yields affords information about the suitability of the amino acid in position P1/