N-Boc-5-bromo-2-fluoro-L-phenylalanine is a Boc-protected phenylalanine analog offering enhanced halogen-based interactions. The residue enables exploration of aromatic stacking, hydrophobic tuning, and electronic effects. Researchers incorporate it into peptides for structural and binding studies.
CAT No: R2107
CAS No:2015412-89-0
Synonyms/Alias:N-Boc-5-bromo-2-fluoro-L-phenylalanine;2015412-89-0;
N-Boc-5-bromo-2-fluoro-L-phenylalanine is a specialty amino acid derivative characterized by the presence of both bromine and fluorine substituents on the aromatic ring, as well as a tert-butyloxycarbonyl (Boc) protecting group on the amino terminus. Its unique structural features make it a valuable building block in modern synthetic chemistry, particularly for peptide research and the development of structurally modified biomolecules. The dual halogenation of the phenylalanine side chain introduces electronic and steric effects that can be exploited for advanced studies in protein engineering, medicinal chemistry, and materials science. As a non-canonical amino acid, it provides researchers with a versatile tool for probing structure-function relationships and for expanding the chemical diversity of peptides and proteins.
Peptide Synthesis: In the field of solid-phase peptide synthesis, N-Boc-5-bromo-2-fluoro-L-phenylalanine serves as an important protected amino acid for the incorporation of halogenated phenylalanine residues into synthetic peptides. The Boc group safeguards the amino functionality during coupling reactions, enabling selective deprotection and sequential assembly of complex peptide chains. Incorporation of this derivative allows for the introduction of site-specific halogenation, which can modulate peptide conformation, stability, and interaction profiles, thereby supporting the creation of novel peptide analogs with tailored properties.
Protein Engineering: The structural modifications present in this compound make it highly suited for use in protein engineering and mutagenesis studies. By substituting standard phenylalanine residues with the bromo- and fluoro-substituted analog, researchers can investigate the effects of altered aromatic side-chain electronics and steric bulk on protein folding, stability, and function. Such substitutions are particularly valuable for mapping ligand-binding sites, studying aromatic interactions, and designing proteins with enhanced or novel functionalities.
Medicinal Chemistry Research: The presence of both bromine and fluorine on the aromatic ring renders this amino acid derivative an attractive scaffold for medicinal chemistry applications, especially in the development of peptide-based drug leads and molecular probes. The halogen atoms can influence binding affinity, metabolic stability, and bioavailability of peptide analogs, facilitating structure-activity relationship (SAR) studies. Additionally, the unique electronic properties imparted by the halogens can be harnessed to create compounds with improved pharmacological profiles for preclinical research.
Bioconjugation and Labeling: The bromo substituent on the aromatic ring provides a reactive handle for further chemical modification through palladium-catalyzed cross-coupling reactions such as Suzuki-Miyaura or Sonogashira couplings. This enables site-specific attachment of various functional groups, fluorescent tags, or affinity labels to peptides and proteins, supporting advanced bioconjugation strategies. Such modifications are instrumental in the development of labeled biomolecules for imaging, target identification, and mechanistic studies in chemical biology.
Analytical Method Development: N-Boc-5-bromo-2-fluoro-L-phenylalanine can also be employed as a reference standard or as a model compound in analytical chemistry for the development and validation of chromatographic and spectroscopic methods. The distinct physicochemical properties conferred by the halogen substituents facilitate method optimization for the detection, quantification, and characterization of halogenated aromatic amino acids and their derivatives in complex mixtures. This application is particularly relevant for laboratories engaged in peptide analysis, quality control, and compound library screening.
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