Ac-L-Trp-NH2 is an N-acetylated L-tryptophan amide in which the indole-containing side chain of tryptophan is retained while the amino terminus is capped with an acetyl group and the carboxyl terminus is converted to a primary amide (-CONH2). The molecule therefore bears an N-acetylated nitrogen, an indole aromatic functionality capable of participating in π-π and hydrogen-bonding interactions, and the amide carbonyl associated with the tryptophan residue, with stereochemistry specified as L at the α-carbon. As a peptide-related intermediate and amino acid derivative, it can be used in peptide synthesis workflows and in chemical biology or analytical studies that require an L-tryptophan unit with a defined terminal amide for conjugation, labeling, or structure-property investigations.
CAT No: CP25647
CAS No:2382-79-8
Synonyms/Alias:2382-79-8;Ac-Trp-NH2;Acetyl-L-tryptophanamide;acetyltryptophanamide;ST057334;(S)-2-Acetamido-3-(1H-indol-3-yl)propanamide;(2S)-2-acetamido-3-(1H-indol-3-yl)propanamide;1H-Indole-3-propanamide,a-(acetylamino)-,(aS)-;Nalpha-acetyltryptophanamide;N-Acetyltryptophanamide;Ac-L-Trp-NH2;N-acetyl-tryptophanamide;2-(Acetylamino)-3-(1H-indol-3-yl)propanamide#;AC1L3RSB;Spectrum2_001346;Spectrum3_001395;Spectrum4_000431;Spectrum5_001632;BSPBio_003010;KBioGR_000782;DivK1c_000359;SCHEMBL455277;SPECTRUM1500699;SPBio_001531;CHEMBL390937
Chemical Name:N-alpha-Acetyl-L-tryptophane amide
Ac-L-Trp-NH2 is an N-acetylated L-tryptophanamide featuring the indole-containing Trp side chain and a C-terminal primary amide, a combination commonly used to model tryptophan residues in peptide-like systems. The acetylated N-terminus and amide functionality provide a defined, proteolysis-relevant end-group environment for chemical biology and peptide chemistry workflows where free amino and carboxyl groups are not desired. This reagent is frequently selected when researchers need a tryptophan-containing building block that behaves as a short, capped peptide fragment for binding, labeling, and analytical studies.
1. Tryptophan Peptide Modeling
Ac-L-Trp-NH2 is used as a capped tryptophan residue mimic in peptide and protein interaction studies, where the indole side chain is the key reporter for local environment effects. Researchers in chemical biology and protein science employ this compound to probe how N- and C-terminal capping influences conformational preferences, solvent exposure, and noncovalent interactions in short peptides or peptide fragments. The acetylated amino terminus and carboxamide at the C-terminus help standardize end-group contributions when comparing Trp-containing sequences or designing peptide analogs.
2. Indole-Driven Binding Studies
Ac-L-Trp-NH2 supports assay development and structure-property experiments that rely on the intrinsic indole characteristics of tryptophan, including environment-dependent fluorescence behavior in many Trp-containing systems. In practice, groups working on receptor/ligand screening, protein-peptide recognition, and binding characterization often use this compound as a defined tryptophanamide to build calibration sets or to generate consistent peptide-like ligands. Its capped termini reduce ambiguity from free functional groups, making it useful for comparing binding responses across series of tryptophan analogs.
3. Analytical Standard Preparation
Ac-L-Trp-NH2 is commonly used as a reference material in analytical workflows that quantify or monitor tryptophan-containing peptide fragments, for example in method development for LC-based assays and peptide profiling. Analytical chemistry and biopharmaceutical research teams use such defined Trp amides to verify retention behavior, support identity confirmation, and establish calibration or qualification materials for small peptide standards. The well-defined acetylated N-terminus and primary amide reduce variability associated with mixtures of free amino acid and carboxylic acid forms.
4. Peptide Library Building Block
Ac-L-Trp-NH2 is applied as a practical tryptophan-containing building block for constructing short peptide analogs and peptide libraries in research settings. Peptide chemistry teams use it to introduce a Trp residue with controlled end-group chemistry, enabling downstream coupling strategies that require a specific N-acetyl and C-amide pattern rather than free termini. This makes the compound useful for generating consistent Trp-containing fragments for subsequent biological testing, materials studies, or mechanistic comparisons in peptide-based chemical biology projects.
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