N-Fmoc-2-fluoro-L-tyrosine introduces a fluorine atom into the tyrosine ring, altering polarity and hydrogen-bonding capacity. Researchers apply it to probe aromatic reactivity, conformational constraints, and modified spectroscopic signatures. Its protected form supports versatile peptide incorporation.
CAT No: R2167
CAS No:1196146-72-1
Synonyms/Alias:N-Fmoc-2-fluoro-L-tyrosine;1196146-72-1;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(2-fluoro-4-hydroxyphenyl)propanoic acid;(S)-2-Fmoc-amino-3-(2-fluoro-4-hydroxyphenyl)propanoic acid;(S)-Fmoc-2-Fluorotyrosine;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(2-fluoro-4-hydroxyphenyl)propanoic acid;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-2-fluoro-L-tyrosine;DTXSID001201439;MFCD30724931;CS-0439176;F80858;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(2-fluoro-4-hydroxyphenyl)propanoic acid;
N-Fmoc-2-fluoro-L-tyrosine is a specialized amino acid derivative widely utilized in peptide chemistry and biochemical research. Structurally, it features a fluoro-substituted tyrosine backbone protected at the N-terminus with a 9-fluorenylmethoxycarbonyl (Fmoc) group, enabling selective incorporation into peptide chains via solid-phase synthesis. The introduction of a fluorine atom at the ortho position of the aromatic ring imparts unique electronic and steric properties, making this compound an invaluable tool for probing structure-function relationships in proteins, developing modified peptides, and advancing studies in chemical biology. Its dual functionality—offering both side-chain modification and temporary N-terminal protection—positions it as a versatile building block for the synthesis of designer biomolecules and the investigation of fluorinated amino acid effects within biological systems.
Peptide Synthesis: N-Fmoc-2-fluoro-L-tyrosine is primarily employed as a protected amino acid monomer in Fmoc-based solid-phase peptide synthesis (SPPS). The Fmoc group provides orthogonal protection, allowing for efficient stepwise elongation of peptide chains while preserving the integrity of the fluoro-tyrosine side chain. Researchers leverage this derivative to introduce site-specific fluorinated residues into peptides, enabling the systematic study of fluorine's influence on peptide stability, folding, and intermolecular interactions. Its compatibility with automated synthesizers and established deprotection protocols streamlines the assembly of complex peptide architectures containing non-canonical amino acids.
Protein Engineering: The incorporation of 2-fluoro-L-tyrosine into recombinant proteins or synthetic peptides offers a strategic approach for modifying physicochemical properties such as hydrophobicity, hydrogen bonding potential, and electronic distribution. By substituting canonical tyrosine residues with the fluorinated analogue, scientists can investigate the impact of subtle side-chain modifications on protein function, ligand binding, and enzymatic activity. This approach is particularly valuable for dissecting aromatic interactions, probing active site dynamics, and engineering proteins with enhanced stability or altered reactivity.
Structural Biology: The unique spectroscopic signatures and altered electronic environment introduced by the fluoro substituent make this amino acid derivative a powerful probe in structural studies. When incorporated into peptides or proteins, it facilitates advanced nuclear magnetic resonance (NMR) and vibrational spectroscopy investigations, allowing researchers to track local conformational changes, monitor site-specific interactions, and map solvent accessibility. The presence of fluorine also enables the use of 19F-NMR, which offers high sensitivity and minimal background signal, thus expanding the analytical toolkit for elucidating biomolecular structure and dynamics.
Chemical Biology: The use of N-Fmoc-2-fluoro-L-tyrosine in chemical biology extends to the development of fluorinated peptide libraries and the design of molecular probes. Its unique chemical reactivity and altered side-chain properties enable the generation of peptides with enhanced resistance to enzymatic degradation or tailored interaction profiles. Such modified peptides serve as valuable tools for target identification, inhibitor screening, and the study of protein-protein interactions within complex biological systems.
Analytical Method Development: The distinct physicochemical characteristics of 2-fluoro-L-tyrosine derivatives support their application in developing and validating analytical methods. These compounds are often utilized as standards or reference materials in chromatographic and mass spectrometric analyses, aiding in the quantification and characterization of fluorinated peptides and proteins. Their defined retention times, fragmentation patterns, and spectroscopic properties facilitate the accurate identification and monitoring of modified biomolecules in diverse research workflows.
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