Carbobenzoxy-L-alanyl-alanyl-asparagine features a protected N-terminus that stabilizes the tripeptide during coupling steps. The mixed residue chemistry supports investigations of hydrogen bonding and early folding events. Researchers use it to model backbone flexibility and side-chain interactions. Applications include synthetic-route optimization and enzymatic specificity studies.
CAT No: R2638
CAS No:499969-23-2
Synonyms/Alias:499969-23-2;SCHEMBL14371944;carbobenzoxy-l-alanyl-alanyl-asparagine;(5S,8S,11S)-11-(2-Amino-2-oxoethyl)-5,8-dimethyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazadodecan-12-oic acid;
Carbobenzoxy-l-alanyl-alanyl-asparagine, also known as Z-Ala-Ala-Asn, is a synthetic tripeptide protected at the N-terminus with a carbobenzoxy (Cbz or Z) group. This compound is widely recognized in peptide chemistry for its utility as a building block in the synthesis of longer peptides and as a model substrate in enzymatic studies. Its stable carbobenzoxy group provides effective protection during peptide coupling reactions, ensuring that the reactive amino group remains shielded from unwanted side reactions. The presence of asparagine at the C-terminus introduces a polar, amide-containing side chain, which is valuable for studying hydrogen bonding and peptide folding. Z-Ala-Ala-Asn's unique sequence and protective group configuration make it a versatile tool in biochemical research, offering precise control over peptide assembly and analysis.
Peptide Synthesis: Carbobenzoxy-l-alanyl-alanyl-asparagine is frequently employed as a protected tripeptide segment in the stepwise synthesis of larger peptides and proteins. The Cbz-protected N-terminus enables selective deprotection and coupling strategies, which are essential for constructing complex peptide sequences with high fidelity. Researchers utilize this tripeptide as a modular unit, integrating it into solid-phase peptide synthesis protocols to streamline the assembly of target molecules. Its use facilitates the efficient incorporation of asparagine residues, which are often challenging due to their side-chain reactivity, thereby enhancing the overall yield and purity of synthesized peptides.
Enzyme Substrate Studies: Z-Ala-Ala-Asn serves as a valuable substrate in enzymatic assays, particularly for investigating the specificity and kinetics of proteases and peptidases. The defined sequence and protective group allow researchers to monitor enzyme-catalyzed hydrolysis events, providing insights into substrate recognition and cleavage mechanisms. By employing this tripeptide in fluorometric or chromatographic assays, scientists can elucidate the preferences of various proteolytic enzymes, supporting the development of selective inhibitors or activity-based probes for biochemical research.
Protein Folding and Structural Analysis: The asparagine residue within Carbobenzoxy-l-alanyl-alanyl-asparagine contributes to studies focused on peptide conformational dynamics and folding mechanisms. Its side chain can participate in hydrogen bonding, mimicking interactions observed in native protein environments. Researchers utilize this tripeptide in spectroscopic and computational studies to model the role of asparagine in stabilizing secondary structures, such as beta turns or loops. These investigations advance the understanding of sequence-structure relationships in peptides and proteins, informing the design of novel biomolecules with tailored properties.
Peptidomimetic Design: The protected tripeptide Z-Ala-Ala-Asn is instrumental in the development of peptidomimetics, which are synthetic analogs designed to mimic the biological activity of natural peptides. By incorporating this sequence into larger scaffolds or modifying its functional groups, chemists can generate compounds with enhanced stability, bioavailability, or target affinity. These peptidomimetics are explored in various research contexts, including the modulation of protein-protein interactions and the creation of molecular probes for cellular studies.
Analytical Method Development: Analytical chemists leverage Carbobenzoxy-l-alanyl-alanyl-asparagine as a calibration standard or reference compound in chromatographic and mass spectrometric methods. Its well-defined structure and predictable fragmentation patterns make it suitable for validating instrument performance and optimizing peptide detection protocols. The tripeptide's use in method development ensures accurate quantification and identification of peptide analytes in complex biological samples, supporting advancements in proteomics and peptide-based analytics.
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