88192-18-1

Usage

Uses

Used in Biochemistry and Molecular Biology:
Azidoalanine is utilized as a protein labeling agent for the purpose of studying protein interactions and reactions. Its incorporation into proteins is facilitated through genetic code expansion techniques, which reassign specific codons to encode the azidoalanine residue. This allows for the subsequent selective modification of the protein via bioorthogonal chemistry, enabling the attachment of probes, fluorophores, or other functional groups for enhanced characterization and analysis.
Used in Proteomics:
In the field of proteomics, azidoalanine is employed as a tool for the comprehensive analysis of proteins within a biological system. Its unique properties allow for the specific tagging and tracking of proteins, aiding in the identification and quantification of various proteins and their interactions within complex biological networks.
Used in Chemical Biology Research:
Azidoalanine is also used as a research tool in chemical biology to explore the mechanisms of protein function and to develop new methods for protein modification and analysis. Its application in this field contributes to the advancement of our understanding of biological processes and the development of novel therapeutic strategies.

Upstream product

• 122225-54-1 (S)-3-azido-2-((tert-butoxycarbonyl)amino)propanoic acid 
• 145967-50-6 benzyl (2S)-3-azido-2-[(tert-butoxycarbonyl)amino]propanoate 
• 76387-70-7 (S)-3-amino-2-tert-butoxycarbonylaminopropionic acid 
• 112839-95-9 (S)-3-amino-2-oxetanone p-toluenesulfonic acid salt 

Relevant academic research and scientific papers

Diaminodiacid-based synthesis of macrocyclic peptides using 1,2,3-triazole bridges as disulfide bond mimetics

A new approach for the efficient construction of 1,2,3-triazole bridges as disulfide surrogates in peptides, utilizing the diaminodiacid strategy was established. Two thanatin derivatives were prepared with 1,5- and 1,4-disubstituted 1,2,3-triazole diaminodiacids as building blocks. The antibacterial activity studies are also described here.

A concise route to L-azidoamino acids: L-azidoalanine, L-azidohomo-alanine and L-azidonorvaline

A simple and highly efficient synthetic route to three homologous azidoamino acids, starting from inexpensive, commercially available, protected natural amino acids is reported. The products can be used to introduce bioorthogonal handles into proteins. Ge

Presentation and detection of azide functionality in bacterial cell surface proteins

An improved protocol for copper-catalyzed triazole formation on the bacterial cell surface is described. Addition of highly pure CuBr to cells treated with azidohomoalanine (2) leads to ca. 10-fold more extensive cell surface labeling than previously observed. This highly active catalyst allows detection of the methionine analogues azidoalanine (1), azidonorvaline (3), and azidonorleucine (4) in cell surface proteins. Azidoalanine was previously believed to be silent with regard to the cellular protein synthesis machinery.

Syntheses of optically pure α-amino acids from 3-amino-2-oxetanone salts

A process for the preparation of optically pure α-amino acids comprising the nucleophilic ring-opening of 3-amino-2-oxetanone salts. N-Protected serine β-lactones are deprotected to form heretofore unknown 3-amino-2-oxetanone and its corresponding salts. In turn these previously unknown 3-amino-2-oxetanone salts may be used in the synthesis of other novel or rare stereochemically-pure free amino acids.