Fmoc-3,5-Dichloro-L-Phenylalanine is a protected amino acid derivative in which the phenylalanine backbone bears two chlorine substituents at the 3 and 5 positions of the aromatic ring, and the amino acid is presented in the L stereochemical form. The molecule contains an Fmoc-protected alpha-amino group and a free carboxylic acid, while the dichloro-substituted benzyl side chain provides a halogenated aromatic functionality that can influence hydrophobicity and electronic character during peptide assembly. In peptide synthesis workflows, the Fmoc group supports stepwise coupling by controlling the reactivity of the amino functionality, and the halogenated side chain is used to introduce chemically distinct aromatic residues for structure-activity studies, chemical biology labeling strategies, or analytical characterization of peptide analogues.
CAT No: CP12506
Fmoc-3,5-Dichloro-L-Phenylalanine is an Fmoc-protected L-phenylalanine derivative bearing two chlorine atoms on the aromatic ring at the 3 and 5 positions. The molecule combines a chiral α-amino acid core with a carbamate-protected N-terminus (Fmoc) and an electron-poor, sterically defined dichlorophenyl side chain that can modulate hydrophobicity, halogen bonding propensity, and aromatic packing. The aryl chlorides are chemically stable under standard peptide coupling conditions yet remain available for downstream transformations such as selective cross-coupling or nucleophilic aromatic substitution after appropriate activation. The compound functions as a stereochemically defined, peptide-compatible building block and as a chiral aromatic intermediate for medicinal chemistry and process-oriented synthesis of halogenated amino acid motifs.
1. Peptide Synthesis
Fmoc-3,5-Dichloro-L-Phenylalanine is used in peptide building workflows where the Fmoc carbamate enables controlled N-terminal deprotection and subsequent amide bond formation at the α-carboxyl functionality. The L-configuration at the α-carbon provides stereochemical fidelity for backbone recognition in solid-phase or solution-phase peptide synthesis, while the dichlorinated phenyl side chain introduces a defined aromatic substitution pattern that can be preserved through coupling and washing cycles. The aromatic chlorides can influence coupling microenvironments and final peptide conformations through halogen effects, supporting the construction of halogenated peptide sequences for structure-focused studies. The resulting peptides and peptide fragments can be carried into downstream purification, fragment elaboration, and analog generation in applied peptide chemistry.
2. Peptidomimetics And SAR
Fmoc-3,5-Dichloro-L-Phenylalanine supports peptidomimetic and SAR-oriented medicinal chemistry by supplying a halogenated phenylalanine motif that can be incorporated into constrained scaffolds and backbone-modified analogs. The Fmoc-protected amino acid form enables stepwise assembly into peptide-like frameworks, while the 3,5-dichloro substitution pattern can be retained to probe structure-function relationships involving aromatic surface area, electronic effects, and intermolecular halogen bonding. The stereodefined amino acid core allows consistent placement of the aromatic side chain relative to the peptide backbone, improving interpretability of analog series. Downstream derivatization can leverage the aryl chlorides for scaffold diversification, enabling access to additional substituted aromatic variants within SAR campaigns.
3. Side-Chain Functionalization
Fmoc-3,5-Dichloro-L-Phenylalanine is suitable for side-chain functionalization strategies that begin with peptide incorporation and proceed to post-assembly aromatic modification. The dichlorinated aromatic ring provides two handles for cross-coupling chemistry or nucleophilic aromatic substitution after appropriate activation, allowing conversion into biaryl, heteroaryl, or substituted phenyl derivatives while maintaining the amino acid backbone stereochemistry. The Fmoc group supports iterative synthetic planning by enabling orthogonal protection logic during assembly, with the aromatic chlorides acting as stable latent electrophiles during peptide coupling steps. The resulting functionalized amino acid derivatives and conjugation-ready intermediates can be used to generate libraries of halogenated and substituted aromatic analogs for chemical biology and synthetic methodology development.
4. Chemical Biology Probes
Fmoc-3,5-Dichloro-L-Phenylalanine can be applied to chemical biology probe construction where halogenated aromatic residues serve as recognition elements in binding studies. The α-amino acid architecture and Fmoc protection support incorporation into peptides, peptide mimics, or protein-interaction modules, while the 3,5-dichlorophenyl side chain can enhance hydrophobic contacts and enable directional halogen interactions with target binding pockets. The stable dichloro substituents help preserve probe integrity during synthesis and purification, supporting the preparation of defined analog sets for receptor or protein-ligand interaction mapping. Downstream probe derivatives may be further elaborated into labeled or immobilizable constructs using the aromatic substitution pattern as a platform for conjugation chemistry.
5. Pharmaceutical Manufacturing Intermediates
Fmoc-3,5-Dichloro-L-Phenylalanine is relevant to pharmaceutical manufacturing and process chemistry as a chiral, protected amino acid intermediate used to prepare halogenated peptide building blocks for active ingredient synthesis. The Fmoc carbamate provides a robust protection strategy compatible with controlled deprotection and coupling operations, supporting reproducible manufacturing routes that require defined stereochemistry and consistent impurity profiles. The dichlorinated aromatic side chain can be carried through manufacturing steps to deliver drug-like halogenated motifs that are difficult to introduce late in synthesis without disrupting peptide integrity. The compound can therefore serve as a feedstock for fine chemical synthesis of protected amino acid derivatives, peptide intermediates, and downstream substituted aromatic variants used in industrial-scale peptide and peptidomimetic production.
6. Analytical Standards and Method Development
Fmoc-3,5-Dichloro-L-Phenylalanine is suitable for analytical research and method development where a defined Fmoc-protected, stereochemically pure amino acid standard supports LC-MS and method validation workflows. The presence of the Fmoc group and the 3,5-dichlorophenyl side chain provides characteristic fragmentation and retention behavior that can be used to track protected amino acid intermediates, monitor coupling-related impurities, and verify identity during peptide synthesis. The stable dichloro aromatic pattern reduces ambiguity when distinguishing closely related phenylalanine derivatives in complex reaction mixtures. The compound can be employed as a reference material for analytical characterization of protected amino acid building blocks, peptide fragments, and halogenated analog series in applied synthetic chemistry.
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