Chloroac-Trp-OH is a tryptophan-based amino acid derivative featuring a chloroacetylated tryptophan residue terminated as a carboxylic acid, placing it in the class of modified amino acids used for peptide and bioconjugation chemistry. The molecule contains an indole side chain characteristic of tryptophan, a free α-amino group and α-carboxyl group, and a chloroacetyl functional handle that can undergo chemoselective reactions with nucleophiles while the aromatic indole remains available for noncovalent interactions in labeling or structural studies. As a protected-free, structurally modified amino acid building block, it is employed in the preparation of peptide-related intermediates and conjugates where the chloroacetyl group provides a reactive electrophile for attaching biomolecular targets under controlled synthetic conditions.
CAT No: CP27323
CAS No:64709-57-5
Synonyms/Alias:Chloroacetyl-L-tryptophan;N-Chloroacetyl-L-tryptophan;64709-57-5;n-(chloroacetyl)-l-tryptophan;L-Tryptophan,N-(chloroacetyl)-(9CI);Chloroacetyltryptophan;Chloroacetyl-Trp-OH;Chloroacetyl-L-Trp-OH;AC1Q3TDI;AC1L2QA9;N-(Chloroacetyl)tryptophan#;BIDD:GT0689;SCHEMBL3194439;CTK5C1626;L-Tryptophan,N-(chloroacetyl)-;PGTJUXHMJYBSBW-NSHDSACASA-N;ZINC1605478;EINECS265-029-5;ANW-34940;AR-1J9909;AKOS015850598;DB-054718;TC-123685;FT-0640967;(2S)-2-(2-chloroacetamido)-3-(1H-indol-3-yl)propanoicacid
Chloroac-Trp-OH is an amino acid derivative built on the tryptophan side chain, retaining the indole aromatic system while presenting a carboxylic acid functionality at the C-terminus and a chlorinated acyl group on the amino terminus (Chloroac). The molecule is chiral at the tryptophan alpha-carbon (depending on the specified stereochemical configuration of the supplied material), and the indole N-H and ring π-system provide distinct electronic and hydrogen-bonding features relevant to peptide recognition and derivatization. The chloroacyl substituent introduces a reactive handle that can participate in acyl transfer chemistry under peptide-synthesis-compatible conditions, while the free carboxylic acid enables conversion to activated esters or amide-forming derivatives for downstream coupling. As a protected/functionalized tryptophan acid building block, Chloroac-Trp-OH is suited for preparing peptide fragments, studying indole-containing motifs, and generating chiral intermediates for synthetic organic chemistry and biochemical research workflows.
1. Peptide Synthesis
Chloroac-Trp-OH supports peptide coupling chemistry in peptide synthesis workflows by combining a carboxylic acid at the tryptophan terminus with an N-acylated amino functionality that can be managed through standard protecting-group strategies. The indole ring can influence coupling and purification behavior, making this building block relevant for constructing Trp-containing sequences where aromatic side-chain stability and controlled reactivity are required. The chlorinated acyl group can be leveraged as a handle for acyl-transfer-compatible transformations or for maintaining N-terminal differentiation during fragment assembly. Downstream, the resulting Trp-containing intermediates can be extended into longer peptide chains or used as defined fragments for structure-activity relationship studies and peptide analog construction.
2. Amino Acid Derivatization
Chloroac-Trp-OH serves as a chiral tryptophan acid intermediate for amino acid derivatization and side-chain-compatible functional transformations. The indole N-H and aromatic π-system enable selective derivatization strategies such as electrophilic substitution or indole-directed conjugation under controlled conditions, while the carboxylic acid can be converted to amide, ester, or activated acid derivatives for scaffold diversification. The N-chloroacyl motif provides a distinct acyl environment that can be retained or modified to tune reactivity during multistep synthesis, including preparation of N-protected amino acid derivatives for orthogonal chemistry. The product can therefore be applied to generate libraries of tryptophan-containing chiral intermediates used in synthetic organic chemistry and biochemical probe development.
3. Chemical Biology Probes
Chloroac-Trp-OH can be employed in chemical biology research to generate indole-bearing probes and peptide-based recognition elements where tryptophan aromatic interactions are central to binding or assay readouts. The indole moiety provides a chemically addressable aromatic functionality for conjugation or incorporation into biomolecule-targeting scaffolds, while the free carboxylic acid supports formation of defined amide linkages to carriers, tags, or linker systems. The N-chloroacyl substitution enables controlled handling of the amino terminus during probe assembly, supporting compatibility with peptide-like coupling steps used to build structured ligands. The resulting Trp-containing constructs can be used as biochemical research intermediates for studying molecular recognition, receptor binding motifs, or enzyme-substrate preferences involving aromatic side chains.
4. Pharmaceutical Intermediate Preparation
Chloroac-Trp-OH is suitable for pharmaceutical intermediate preparation in fine chemical synthesis routes that require a chiral tryptophan-derived building block with a differentiated N-acyl group and a coupling-ready carboxylic acid. The combination of an indole aromatic side chain and a functionalized amino terminus supports incorporation into peptide-like intermediates used in drug discovery chemistry, including peptidomimetic scaffolds and constrained aromatic amino acid motifs. The chlorinated acyl group can be managed as part of a protecting-group strategy to control chemoselectivity during stepwise assembly and to enable downstream conversion into activated derivatives for amide bond formation. The compound thereby functions as a process-relevant intermediate for manufacturing-oriented synthesis planning where defined stereochemistry and functional-group compatibility are required.
5. Analytical Research Standards
Chloroac-Trp-OH can be applied in analytical research as a reference material and derivatization precursor for quantifying tryptophan-containing fragments and monitoring peptide coupling outcomes. The presence of a stable indole chromophore and a carboxylic acid group supports detectability in chromatographic and spectroscopic methods, while the N-chloroacyl functionality provides a distinguishable chemical signature for method development. The defined amino acid derivative form can be used to generate calibration standards, internal standards, or structurally matched analogs that reflect N-terminal acylation states in peptide synthesis. The ability to access consistent Trp-containing structures makes it relevant for quality control of peptide building blocks, impurity profiling, and analytical method validation in amino acid and peptide chemistry workflows.
1. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review
5. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More