82611-57-2

Usage

Molecular structure

Contains a benzyloxycarbonyl group and a 4-bromophenyl group attached to a propanoic acid molecule.

Derivative

Is a derivative of propanoic acid.

Usage

Often used in organic synthesis and medicinal chemistry.

Protecting group

Benzyloxycarbonyl group is commonly used as a protecting group for amines in organic synthesis.

Pharmaceutical and agrochemical compounds

4-bromophenyl group is often found in pharmaceutical compounds and agrochemicals.

Potential applications

Could have potential applications in the development of new drugs or other bioactive molecules due to its structure and reactivity.

Upstream product

• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 141971-13-3 Z-DL-Phe(4Br)OMe 
• 187028-22-4 Z-DL-Phe(4Br)-OCH₂CF₃ 
• 14091-15-7 p-bromo-DL-phenylalanine 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 141971-13-3 Z-DL-Phe(4Br)OMe 
• 187028-22-4 Z-DL-Phe(4Br)-OCH₂CF₃ 
• 1021733-85-6 benzyl {1-(4-bromobenzyl)-2-[(2-hydroxy-4,4-dimethylhexyl)amino]-2-oxoethyl}carbamate 

Relevant academic research and scientific papers

SUBSTITUTED IMIDAZOLES AS BOMBESIN RECEPTOR SUBTYPE-3 MODULATORS

Certain novel substituted imidazoles are ligands of the human bombesin receptor and, in particular, are selective ligands of the human bombesin receptor subtype-3 (BRS-3). They are therefore useful for the treatment, control, or prevention of diseases and disorders responsive to the modulation of BRS-3, such as obesity, and diabetes.

Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.

α-chymotrypsin-catalysed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in organic solvents with low water content: Incorporation of non-protein amino acids into peptides

The α-chymotrypsin-catalyzed peptide synthesis via the kinetically controlled approach using activated esters as acyl donors in orgnanic solvents with low water content was presented. The methyl esters of N-Z derivatives of racemic non-protein amino acids were chosen as carboxy components. They allowed the peptide-bond formation and optical resolution simultaneously to yield homochiral peptides. This method is useful for the incorporation of non-protein amino acids into peptides.

α-Chymotrypsin-catalysed peptide synthesis using activated esters as acyl donors

The coupling efficiency in α-chymotrypsin-catalysed peptide synthesis is greatly improved by the use of activated esters such as the 2,2,2-trifluoroethyl ester as acyl donor instead of the conventional methyl ester; this approach is useful for the incorporation of non-protein amino acids into peptides.