Fmoc-3,5-Dichloro-D-Phenylalanine is a protected amino acid derivative of D-phenylalanine bearing two chlorine substituents on the aromatic ring at the 3- and 5-positions. The molecule contains an Fmoc-protected amino group and a free carboxylic acid, with the side chain functioning as a chlorinated phenyl moiety that can influence hydrophobicity and aromatic interactions in peptide frameworks. In peptide synthesis workflows, the Fmoc group supports stepwise assembly by enabling controlled deprotection while the D-configuration and halogenated aromatic side chain provide a defined steric and electronic pattern for structure-activity studies and analog incorporation.
CAT No: CP12507
Fmoc-3,5-Dichloro-D-Phenylalanine is a chiral, N-(9H-fluoren-9-ylmethoxycarbonyl) protected D-phenylalanine derivative bearing two chlorine atoms at the 3,5-positions of the aromatic ring. The molecule combines an Fmoc-protected amino group for orthogonal peptide coupling with a stereodefined α-carbon from the D-configuration, while the dichloro-substituted phenyl side chain provides increased hydrophobicity and modulates electronic properties through halogen substitution. The aryl chlorides are chemically stable under many peptide synthesis conditions yet can participate in downstream substitution or cross-coupling chemistry after peptide assembly or side-chain derivatization. The compound functions as a protected amino acid building block and chiral intermediate for constructing halogenated peptide motifs and related peptidomimetic scaffolds.
1. Peptide Synthesis
Fmoc-3,5-Dichloro-D-Phenylalanine is used in solid-phase peptide synthesis and solution-phase peptide coupling where the Fmoc group enables controlled N-terminal deprotection and subsequent amide bond formation. The protected amino acid derivative presents a stereodefined D-α-amino acid center and a halogenated phenyl side chain that can be incorporated as a single residue to tune conformational preferences and hydrophobic contacts in peptide sequences. The 3,5-dichloro substitution can help preserve side-chain integrity during coupling and deprotection steps while remaining available for later functionalization after assembly. Halogenated D-phenylalanine-containing peptides prepared from this building block can be applied to peptide library generation, structural studies, and scaffold optimization in peptide science.
2. Peptidomimetics And SAR Studies
Fmoc-3,5-Dichloro-D-Phenylalanine supports peptidomimetic construction and structure-activity relationship studies by introducing a D-amino acid stereocenter and a dichloroaryl pharmacophore-like motif into peptide analogs. The Fmoc-protected amine allows stepwise synthesis of analog series, while the electron-withdrawing chlorines at the 3,5-positions can influence aromatic ring interactions, local polarity, and potential binding-site fit in SAR workflows. The resulting halogenated residue can be retained as a stable hydrophobic handle or used as a platform for further derivatization to probe substituent effects. Downstream analogs derived from this building block can serve as chemically defined research intermediates for SAR mapping and medicinal chemistry-style optimization of peptide-like structures.
3. Side-Chain Functionalization Chemistry
Fmoc-3,5-Dichloro-D-Phenylalanine is suitable for synthetic organic chemistry routes that leverage aryl chloride reactivity for post-assembly diversification. The dichloro-substituted phenyl side chain provides two positions that may undergo nucleophilic aromatic substitution or transition-metal-catalyzed cross-coupling after peptide synthesis, enabling attachment of solubilizing groups, affinity handles, or reporter moieties. The Fmoc-protected amino acid format supports incorporation into peptides or protected intermediates before selective side-chain transformation, which can be advantageous when orthogonality between backbone chemistry and aromatic functionalization is required. Halogen-to-substituent conversion strategies starting from this residue can generate functionalized peptide fragments, conjugation-ready intermediates, and chemically tractable building blocks for downstream synthesis.
4. Chemical Biology And Biomolecule Labeling
Fmoc-3,5-Dichloro-D-Phenylalanine can be employed in chemical biology workflows that require incorporation of halogenated D-amino acid residues into peptides used as recognition elements or labeling probes. The protected amino group enables precise installation of the residue at defined positions, while the D-configuration can affect protease stability and conformational behavior of the resulting peptide probe. The 3,5-dichloro phenyl group can act as a chemically addressable handle for subsequent conjugation chemistry, including attachment of linkers or tags via aromatic substitution/coupling after the peptide is assembled. Labeled or derivatized peptide constructs prepared from this building block can be used as research reagents for studying molecular interactions, mapping binding interfaces, and generating defined biomolecule-associated probes.
5. Pharmaceutical Intermediate Preparation
Fmoc-3,5-Dichloro-D-Phenylalanine is applicable to pharmaceutical intermediate preparation where protected amino acid derivatives are manufactured for controlled incorporation into peptide-like active ingredients or process intermediates. The Fmoc-protection strategy supports reproducible peptide coupling chemistry in downstream manufacturing steps, while the stereochemically defined D-phenylalanine center provides consistent stereochemical outcomes across synthetic batches. The dichloroaryl side chain can be carried through protected stages due to its stability under typical peptide synthesis conditions, then transformed to meet formulation or property requirements through later functional group interconversions. This makes the compound relevant to fine chemical synthesis and process chemistry intermediate supply chains that produce halogenated peptide building blocks for research and industrial manufacturing contexts.
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