H-D-Trp(For)-OH*HCl is a hydrochloride salt form of a deuterated tryptophan derivative bearing a formyl (For) substituent on the indole ring, classed as an amino acid analogue used in chemical labeling and peptide-related studies. The molecule contains a deuterated amino acid backbone with an amino functional group and a carboxyl group present as a salt, while the indole side chain is modified by the formyl substituent that alters hydrogen-bonding and aromatic reactivity; stereochemistry is not specified in the name. As an amino acid derivative, it is employed as a labeled building block or substrate analogue in synthetic peptide workflows and analytical method development where indole-functionalized, isotopically differentiated tryptophan residues are required.
CAT No: CP25802
CAS No:367453-01-8
Synonyms/Alias:H-D-Trp(For)-OHHCl;367453-01-8;H-D-TRP-OHHCL;7123AH
Chemical Name:N-in-Formyl-D-tryptophan hydrochloride
H-D-Trp(For)-OH*HCl is a hydrochloride salt form of a D-configured tryptophan derivative bearing a formyl-protected indole substituent (For) on the indole nitrogen/side functionality, while retaining the amino acid backbone as a carboxylic acid (OH) and an N-terminus suitable for peptide chemistry after appropriate activation. The D stereocenter at the alpha carbon provides defined stereochemical control for incorporation into D-peptides and stereochemically constrained analogs. The indole ring contributes aromatic π-systems for molecular recognition and can participate in electrophilic and oxidative transformations under controlled conditions, while the protected indole functionality modulates reactivity during coupling and subsequent deprotection. The salt form improves handling and can influence solubility in polar media, supporting its use as a chiral amino acid intermediate and protected peptide building block in synthetic workflows.
1. D-Peptide Synthesis
H-D-Trp(For)-OH*HCl supports peptide synthesis workflows focused on D-amino acid incorporation, where the D-tryptophan stereochemistry enables access to D-peptide backbones and stereochemically defined peptide analogs. The amino acid carboxylic acid and alpha-amino functionality can be converted into coupling-ready forms, while the formyl-protected indole functionality helps suppress premature indole side reactions during amide bond formation. Indole aromaticity remains available for downstream functionalization after deprotection, enabling construction of peptide scaffolds with controlled aromatic presentation. The resulting D-tryptophan-containing peptide fragments can be applied to studies of protease resistance, conformational effects, and stereochemical structure-property relationships in peptide science.
2. Peptidomimetic Building Blocks
H-D-Trp(For)-OH*HCl serves as a chiral tryptophan-derived building block for peptidomimetic construction and fragment assembly in synthetic organic chemistry. The protected indole functionality allows the indole to be handled as a masked reactive site during scaffold assembly, while the amino acid backbone provides a defined geometry for subsequent coupling into larger structures. Indole's aromatic and heteroatom features can be leveraged for noncovalent interactions in molecular design, including π-stacking and hydrogen-bonding motifs after appropriate deprotection or functional group transformation. Downstream derivatives can be generated for medicinal chemistry-style library synthesis, SAR studies, and conformationally constrained analog development using amino acid chemistry principles.
3. Protected Amino Acid Chemistry
H-D-Trp(For)-OH*HCl is suitable for protected amino acid synthesis strategies where indole functionality requires temporary masking to maintain chemoselectivity. The formyl-protected indole component functions as a protecting-group element that can be removed or transformed under conditions compatible with peptide coupling sequences, helping prevent undesired indole oxidation, electrophilic substitution, or side-chain cross-reactions. The D configuration at the alpha carbon provides stereochemical fidelity through multi-step syntheses, supporting the preparation of stereochemically defined chiral intermediates for peptide building block preparation. The hydrochloride salt form can support reproducible handling during derivatization, making the compound applicable to route design for protected amino acid intermediates used in fine chemical and peptide manufacturing contexts.
4. Chemical Biology Labeling
H-D-Trp(For)-OH*HCl can be applied in chemical biology research where tryptophan-containing motifs are used as anchors for labeling, probe construction, or affinity-based tagging. The amino acid backbone enables incorporation into peptide conjugates or biomolecule-reactive intermediates, while the indole aromatic system can support spectroscopic readouts and interaction-based detection depending on the final labeling format. The protected indole functionality helps maintain integrity during conjugation steps, allowing controlled unveiling or further derivatization after the conjugate is assembled. Resulting labeled peptides or peptide-like probes can be used to interrogate biomolecular binding, monitor molecular interactions, and generate analytical standards for studies of amino acid incorporation patterns and stereochemical effects.
5. Pharmaceutical Intermediate Preparation
H-D-Trp(For)-OH*HCl fits pharmaceutical intermediate preparation workflows that require chiral amino acid derivatives for synthesis of peptide-like active ingredients, peptidomimetics, or process intermediates. The presence of a carboxylic acid and a D-configured alpha stereocenter supports conversion into activated derivatives for controlled coupling steps in manufacturing-oriented synthetic sequences. The formyl-protected indole functionality can be used to manage chemoselectivity across multi-functional molecules, reducing side reactions that would otherwise complicate purification and downstream transformations. The compound's role as a protected, stereodefined tryptophan intermediate enables scalable fine chemical synthesis of complex nitrogen-containing scaffolds and supports industrial chemical manufacturing routes for amino acid-derived products.
6. Analytical Research Standards
H-D-Trp(For)-OH*HCl can be employed as an analytical research standard and reference material in methods development for amino acid derivative characterization. The distinct D stereochemistry and protected indole functionality provide a defined chemical identity that can be used to validate chromatographic behavior, mass spectrometric fragmentation patterns, and derivatization compatibility for amino acid analysis. The hydrochloride salt form can help standardize sample preparation in polar solvents, supporting reproducible analytical workflows for monitoring protected amino acid building blocks and their deprotected or coupled forms. Analytical use can extend to quality control of peptide synthesis intermediates, stereochemical integrity checks in D-amino acid incorporation, and method verification for amino acid derivatization chemistry in research and industrial settings.
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