This heavily halogenated D-phenylalanine analog offers unique electronic and steric properties for peptide modification. The Fmoc protection facilitates incorporation into solid-phase synthesis. Researchers use it to study halogen bonding, aromatic interactions, and conformational effects. Its dual-halogen pattern enhances mechanistic probing.
CAT No: R2106
CAS No:2015413-31-5
Synonyms/Alias:N-Fmoc-5-bromo-2-chloro-D-phenylalanine;2015413-31-5;
N-Fmoc-5-bromo-2-chloro-D-phenylalanine is a synthetic derivative of D-phenylalanine featuring both 5-bromo and 2-chloro substitutions on the aromatic ring, and protected at the N-terminus with a fluorenylmethoxycarbonyl (Fmoc) group. As an Fmoc-protected, non-canonical amino acid, it is primarily valued in peptide chemistry for its ability to introduce unique halogenated aromatic functionalities into peptide backbones. The strategic incorporation of such halogenated residues enables researchers to explore new chemical space within peptide sequences, facilitating investigations into structure-activity relationships, molecular recognition, and the development of advanced peptide-based materials. Its distinct stereochemistry and functional group profile make it an important tool for expanding the diversity and utility of synthetic peptides in modern biochemical research.
Peptide Synthesis: N-Fmoc-5-bromo-2-chloro-D-phenylalanine is widely utilized as a building block in solid-phase peptide synthesis (SPPS). The Fmoc protecting group ensures compatibility with standard Fmoc-based protocols, allowing for efficient incorporation of the halogenated D-phenylalanine residue into growing peptide chains. The presence of both bromo and chloro substituents on the aromatic ring offers chemists the opportunity to design peptides with enhanced steric and electronic properties, supporting the creation of novel sequences that can be tailored for specific biophysical or functional studies.
Structure-Activity Relationship Studies: The introduction of halogen atoms into the phenylalanine side chain provides a powerful means to modulate peptide conformation and interaction profiles. By incorporating N-Fmoc-5-bromo-2-chloro-D-phenylalanine into model peptides, researchers can systematically investigate the effects of halogenation and D-stereochemistry on biological recognition, binding affinity, and resistance to enzymatic degradation. Such studies are essential for optimizing lead compounds in peptide drug discovery and for probing the molecular determinants of protein-peptide interactions.
Site-Specific Labeling and Functionalization: The bromo and chloro substituents present on the aromatic ring serve as orthogonal handles for post-synthetic modification. Through selective cross-coupling reactions, such as Suzuki or Buchwald-Hartwig couplings, these halogenated sites can be further functionalized to introduce probes, tags, or other chemical moieties. This enables the creation of multifunctional peptides for use in imaging, affinity purification, or mechanistic studies, greatly expanding the utility of the parent peptide scaffold.
Development of Peptidomimetics: The D-configuration of this amino acid, combined with its halogenated aromatic ring, makes it a valuable component in the design of peptidomimetics and constrained peptide analogs. Incorporation of N-Fmoc-5-bromo-2-chloro-D-phenylalanine can enhance metabolic stability and modulate peptide backbone conformation, supporting the development of bioactive molecules with improved pharmacokinetic or biophysical properties. Researchers leverage these features to generate peptide analogs with altered receptor selectivity or resistance to proteolytic enzymes.
Analytical Method Development: The unique mass and electronic properties imparted by the bromo and chloro substituents facilitate the use of peptides containing this residue as analytical standards or probes. Such modified peptides can be employed in mass spectrometry-based assays to improve detection sensitivity or to study peptide fragmentation patterns. Additionally, the distinctive chromophoric characteristics of the Fmoc group and the halogenated aromatic ring can aid in the development of chromatographic or spectroscopic methods for peptide analysis and quality control.
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