Fmoc-2,4-Dichloro-L-Phenylalanine is an Fmoc-protected amino acid derivative in which the phenylalanine side chain bears two chlorine substituents at the 2- and 4-positions, forming a substituted aromatic residue for peptide construction. The molecule contains an Fmoc carbamate protecting the α-amino group and a free carboxylic acid for coupling, while the side chain retains a benzylic methylene linked to the dichlorophenyl ring and is specified as the L stereochemical form at the α-carbon. This protected analogue is used in peptide synthesis workflows, including solid-phase peptide synthesis, where the Fmoc group controls chemoselectivity during stepwise assembly and the 2,4-dichloro substitution provides a defined hydrophobic and halogenated aromatic functionality for structure-activity and chemical biology studies.
CAT No: CP12106
Fmoc-2,4-Dichloro-L-Phenylalanine is an Fmoc-protected L-phenylalanine derivative bearing two chlorine substituents on the aromatic ring at the 2- and 4-positions. The molecule combines an N-(9H-fluoren-9-ylmethoxycarbonyl) protecting group on the amino functionality with a stereodefined L-α-carbon and a side-chain carboxyl group that is available for peptide coupling after standard activation. The dichloro-substituted phenyl ring increases hydrophobicity and modulates electronic properties, which can influence amide formation kinetics and the conformational preferences of resulting peptides. The aryl chlorides are chemically stable under typical peptide synthesis conditions yet can serve as handles for later derivatization or cross-coupling-based diversification, making the compound a chiral, protected amino acid intermediate for structure-guided synthesis.
1. Peptide Synthesis
Fmoc-2,4-Dichloro-L-Phenylalanine is used in solid-phase peptide synthesis and solution-phase peptide assembly where Fmoc chemistry enables controlled N-deprotection and sequential chain elongation. The Fmoc group provides orthogonal protection to the amino functionality, while the L-configuration at the α-carbon preserves stereochemical integrity during coupling steps. The side-chain remains aligned with standard peptide coupling strategies after activation, allowing incorporation into peptide building blocks that contain aryl-rich pharmacophore elements. The dichloro-phenyl side chain can be retained through synthesis to generate peptides with defined hydrophobic and steric characteristics for downstream characterization and analog generation. Product Application in peptide chemistry is supported by the stability of the aryl chlorides under routine deprotection and coupling conditions, enabling consistent scaffold construction for research-grade peptide libraries.
2. Peptidomimetics And SAR Studies
Fmoc-2,4-Dichloro-L-Phenylalanine is applied in peptidomimetic construction and structure-activity relationship studies where aromatic substitution patterns are used to tune binding-site interactions. The dichloro substitution at the 2- and 4-positions introduces controlled steric bulk and electron-withdrawing effects relative to unsubstituted phenylalanine, which can alter conformational behavior and intermolecular recognition in peptide-like scaffolds. The Fmoc-protected L-amino acid format supports systematic incorporation into analog series while maintaining stereochemical fidelity at the chiral center. The retained aryl chlorides can be leveraged for later diversification to generate additional analogs for SAR workflows without changing the backbone stereochemistry. This amino acid derivative therefore functions as a chiral, protected intermediate for medicinal chemistry-oriented scaffold expansion and side-chain electronic tuning.
3. Side-Chain Functionalization
Fmoc-2,4-Dichloro-L-Phenylalanine is suitable for side-chain functionalization strategies that exploit aryl chloride reactivity after peptide assembly or intermediate conversion. The dichloro-substituted aromatic ring can undergo chemoselective transformations such as nucleophilic aromatic substitution or transition-metal-catalyzed cross-coupling to introduce heterocycles, aryl groups, or solubilizing substituents while leaving the peptide backbone intact. The Fmoc-protected amino acid format enables incorporation into protected peptide fragments, followed by deprotection and selective downstream modification at the chlorinated positions. The stereodefined L-phenylalanine core ensures that functionalization proceeds without scrambling the α-chiral center, which is critical for reproducible structure-function studies. Industrially, this approach aligns with fine chemical synthesis routes that require stable protected intermediates for controlled late-stage diversification of aromatic motifs.
4. Chemical Biology Probes
Fmoc-2,4-Dichloro-L-Phenylalanine is used in chemical biology and molecular probe synthesis where defined aromatic substitution supports binding selectivity and probe stability. The Fmoc group allows efficient incorporation into peptide tags or probe scaffolds, while the L-configuration supports consistent stereochemical presentation to biological targets. The dichloro-phenyl side chain can contribute to hydrophobic contacts and can serve as a platform for subsequent conjugation chemistry when converted to more reactive aryl derivatives. The aryl chlorides can be retained during initial scaffold assembly and then transformed to introduce affinity handles, reporter motifs, or clickable groups for downstream labeling workflows. This makes the compound compatible with peptide-based probe construction and amino acid derivatization strategies used to generate chemically defined reagents for biochemical investigation.
5. Pharmaceutical Intermediate Preparation
Fmoc-2,4-Dichloro-L-Phenylalanine is relevant to pharmaceutical intermediate preparation and process chemistry for the manufacture of peptide-based building blocks and chiral aromatic amino acid derivatives. The Fmoc-protected amine provides a robust handle for controlled N-protection during multi-step synthesis, supporting scalable peptide coupling operations and minimizing side reactions associated with free amines. The dichloro aromatic functionality offers a stable, late-stage derivatization site that can be carried through manufacturing steps and converted to alternate substituents during downstream intermediate formation. The stereodefined L-α-carbon supports reproducible quality in chiral synthesis, which is important for consistent performance of downstream peptide intermediates. The compound thereby serves as a chiral, protected amino acid intermediate for industrial chemical manufacturing routes that require both protection control and functional-group retention for later diversification.
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
5. Emerging applications of nanotechnology for diagnosis and therapy of disease: a review
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