N-Fmoc-5-bromo-2-chloro-L-phenylalanine carries dual halogenation on the aromatic ring, providing strong steric and electronic modifications. The residue aids investigations into halogen bonding, hydrophobic clustering, and π-π perturbation. Researchers use it for tuning aromatic interactions and designing specialized peptidomimetics. Its Fmoc group enables reliable synthetic incorporation.
CAT No: R2118
CAS No:2002401-84-3
Synonyms/Alias:N-Fmoc-5-bromo-2-chloro-L-phenylalanine;2002401-84-3;(2S)-3-(5-bromo-2-chlorophenyl)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}propanoic acid;SCHEMBL25657520;F80978;(2S)-3-(5-bromo-2-chlorophenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoic acid;
N-Fmoc-5-bromo-2-chloro-L-phenylalanine is a synthetically modified amino acid derivative featuring both bromine and chlorine substitutions on the aromatic ring of L-phenylalanine, protected at the amino group with a fluorenylmethyloxycarbonyl (Fmoc) moiety. This compound is primarily utilized in the field of peptide chemistry, where its unique halogenated structure imparts valuable chemical versatility for advanced research applications. The presence of electron-withdrawing halogens on the phenyl ring not only alters the electronic properties of the amino acid but also enables site-specific functionalization, making it a significant building block in the design of structurally diverse peptides and modified biomolecules. Its compatibility with standard solid-phase peptide synthesis (SPPS) protocols further enhances its utility for researchers seeking to incorporate non-canonical amino acids into peptide sequences for structure-activity studies or the creation of novel biomaterials.
Peptide Synthesis: As an Fmoc-protected amino acid, N-Fmoc-5-bromo-2-chloro-L-phenylalanine is ideally suited for use in solid-phase peptide synthesis. The Fmoc group provides orthogonal protection, allowing for sequential assembly of peptide chains under mild deprotection conditions. The halogenated aromatic side chain enables the introduction of electron-deficient aromatic residues into target peptides, which can profoundly influence peptide folding, stability, or interaction profiles. Researchers employ this derivative to systematically investigate the effects of aromatic substitution on peptide structure and function, facilitating the rational design of peptides with tailored physicochemical properties.
Structure-Activity Relationship Studies: The incorporation of 5-bromo-2-chloro substitutions on the phenylalanine side chain offers a powerful tool for probing the role of aromatic residues in protein-peptide interactions. By substituting native phenylalanine with this halogenated analog, scientists can assess the impact of altered steric and electronic environments on binding affinity, molecular recognition, and biological activity in receptor-ligand systems. Such studies are critical for the development of peptide-based modulators, inhibitors, or molecular probes with enhanced selectivity and potency.
Chemical Diversification and Conjugation: The bromine and chlorine atoms present on the aromatic ring serve as strategic handles for further chemical modification via cross-coupling reactions such as Suzuki, Sonogashira, or Buchwald-Hartwig methodologies. This enables the post-synthetic introduction of a wide range of functional groups, fluorescent tags, or bioconjugation partners at defined positions within a peptide or protein. The ability to site-specifically derivatize peptides expands opportunities for the creation of multifunctional biomolecules, imaging agents, or affinity reagents for advanced biochemical and analytical applications.
Biophysical and Conformational Analysis: Incorporation of halogenated phenylalanine derivatives into peptides allows researchers to study the influence of aromatic substitution on secondary structure, folding dynamics, and aggregation behavior. The altered electronic and steric properties of the side chain can modulate π-π stacking, hydrophobic interactions, and overall molecular conformation. Such investigations are essential for elucidating the principles governing peptide self-assembly, stability, and intermolecular interactions, informing the design of peptides with desired structural or functional attributes.
Analytical Method Development: The distinct mass and spectroscopic signatures conferred by bromine and chlorine atoms make this amino acid derivative a valuable internal standard or probe in mass spectrometry and chromatographic analyses. Its unique isotopic pattern facilitates the unambiguous identification and quantitation of peptides incorporating this residue, aiding in the characterization of synthetic products, mapping of modification sites, and validation of peptide purity in research workflows. The compound's utility in analytical method development supports rigorous quality control and structural verification in peptide chemistry laboratories.
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