Fmoc-2,6-Dichloro-L-Phenylalanine is an Fmoc-protected, non-natural amino acid derivative in which the phenylalanine side chain bears two chlorine substituents at the 2- and 6-positions of the aromatic ring. The molecule contains a free carboxyl group and an Fmoc-protected amino group, with the side chain functioning as a substituted aryl moiety that can influence hydrophobicity and steric profile relative to unsubstituted phenylalanine while retaining the L stereochemical designation indicated in the name. As a protected building block for peptide synthesis, it can be incorporated into peptide chains under stepwise coupling conditions while the Fmoc group provides orthogonal control of the amino functionality and the dichloro aromatic ring supports structure-activity studies, binding-site probing, and conformational or interaction mapping in chemical biology workflows.
CAT No: CP12306
Fmoc-2,6-Dichloro-L-Phenylalanine is an Fmoc-protected L-phenylalanine derivative bearing two chlorine atoms at the 2- and 6-positions of the aromatic ring. The molecule combines a stereochemically defined α-amino acid framework with an Fmoc carbamate that supports controlled N-protection for solid-phase peptide synthesis, while the dichloro-substituted phenyl side chain introduces increased hydrophobicity and distinct electronic effects. The aryl chlorides are chemically stable under standard peptide coupling conditions yet remain functional handles for later transformations such as selective cross-coupling or nucleophilic aromatic substitution, depending on the downstream chemistry. The resulting chiral amino acid building block is suited to peptide construction and medicinal chemistry-oriented derivatization where aromatic halogenation and protected amino acid compatibility are both required.
1. Peptide Synthesis
Fmoc-2,6-Dichloro-L-Phenylalanine is applied in peptide building block preparation for both research-scale and manufacturing-oriented solid-phase peptide synthesis. The Fmoc-protected α-amino group enables routine deprotection and subsequent peptide coupling, while the L-configuration preserves stereochemical fidelity at the amino acid residue level. The 2,6-dichloro phenyl side chain can be incorporated to modulate aromatic packing, steric profile, and local hydrophobic interactions within peptide sequences. Downstream peptide analogs prepared from this residue can serve as scaffold elements in sequence optimization, linker studies, and structure-directed peptide design, with the halogenated aromatic ring providing a handle for later functional diversification.
2. Peptidomimetics And SAR
Fmoc-2,6-Dichloro-L-Phenylalanine supports peptidomimetic construction and structure-activity relationship studies in medicinal chemistry workflows. The dichloro-substituted aromatic ring contributes defined electronic and steric characteristics that can be retained in peptide analogs or incorporated into constrained mimetics, while the Fmoc group allows systematic assembly of multi-residue libraries. The protected amino acid format facilitates parallel synthesis of analog series where aromatic halogen patterning is varied across positions to probe binding site tolerance. Resulting products can be carried forward as SAR-focused intermediates and molecular design elements, enabling targeted exploration of how halogen substitution influences conformation and intermolecular recognition.
3. Side-Chain Functionalization
Fmoc-2,6-Dichloro-L-Phenylalanine is utilized for side-chain functionalization strategies where aryl chloride substituents act as synthetic handles after peptide or intermediate assembly. The amino acid backbone provides a stable residue for incorporation into protected peptide fragments, while the 2,6-dichloro aromatic ring can undergo further synthetic transformations such as palladium-catalyzed cross-coupling or other aryl chloride activation chemistries during downstream diversification. The presence of two ortho chlorides can also influence regioselectivity and steric accessibility in subsequent derivatization steps. Functionalized derivatives derived from this residue can be used to generate libraries of aromatic substituents for chemical biology probes, binding studies, and fine chemical synthesis routes that require controlled introduction of aryl substituents.
4. Chemical Biology Probes
Fmoc-2,6-Dichloro-L-Phenylalanine is suitable for chemical biology research requiring halogenated aromatic residues in probe molecules and affinity reagents. The Fmoc-protected amino acid framework supports incorporation into peptides and peptide-like constructs used for target engagement studies, while the dichloro phenyl side chain can enhance hydrophobic contacts and provide discrete sites for later conjugation or labeling through aromatic functionalization. The defined L-stereochemistry helps maintain consistent conformational behavior across probe variants, supporting structure-controlled interpretation of binding or recognition outcomes. Downstream probe generation can include peptide conjugates, tagged fragments, and derivatized scaffolds where aromatic halogen chemistry enables controlled access to additional functional groups.
5. Pharmaceutical Intermediate Preparation
Fmoc-2,6-Dichloro-L-Phenylalanine is relevant to pharmaceutical intermediate preparation and specialty chemical production where protected amino acid intermediates are required for controlled synthesis of halogenated peptide analogs. The Fmoc carbamate provides a robust N-protection strategy compatible with standard peptide coupling and deprotection logic, enabling manufacturing-friendly sequence assembly of defined chiral residues. The dichloro-substituted phenyl group can be carried through intermediate steps to maintain a specific aromatic substitution pattern that may be required in downstream active or preclinical candidate synthesis. Resulting intermediates can be used to support process chemistry development for halogenated peptidomimetics, fragment building blocks, and controlled synthesis of multi-functional molecules in industrial chemical manufacturing settings.
6. Analytical Standards and Method Development
Fmoc-2,6-Dichloro-L-Phenylalanine can be employed in analytical research for method development and reference standard generation related to amino acid derivatives and peptide fragments. The combination of an Fmoc-protected amino acid structure with a distinctive 2,6-dichlorophenyl side chain yields a characteristic mass signature and chromatographic behavior that can aid identification and quantification in LC-MS and related workflows. The stereodefined L-amino acid core supports unambiguous assignment of residue-derived peaks in peptide analysis, while the protected functional group enables consistent handling during analytical sample preparation. Analytical standards prepared from this building block can support impurity profiling, stability studies of protected amino acid intermediates, and verification of peptide coupling outcomes during research and industrial manufacturing development.
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