N-Fmoc-O-(trifluoromethyl)-L-tyrosine introduces a strongly electron-withdrawing group to the tyrosine ring. The modification alters polarity, aromaticity, and hydrogen-bonding potential. Researchers use it to study fluorine-driven interactions and modified spectroscopic signatures. Its Fmoc protection aids precise incorporation.
CAT No: R2113
CAS No:1260614-87-6
Synonyms/Alias:N-Fmoc-O-(trifluoromethyl)-L-tyrosine;1260614-87-6;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(4-(trifluoromethoxy)phenyl)propanoic acid;FMOC-TYR(CF3)-OH;(2S)-2-{[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]AMINO}-3-[4-(TRIFLUOROMETHOXY)PHENYL]PROPANOIC ACID;Fmoc-L-Phe(4-OCF3)-OH;SCHEMBL25178687;Fmoc-O-(trifluoromethyl)-L-tyrosine;MFCD07371983;CS-0357471;F80042;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-[4-(trifluoromethoxy)phenyl]propanoic acid;
N-Fmoc-O-(trifluoromethyl)-L-tyrosine is a synthetic amino acid derivative featuring a fluorenylmethyloxycarbonyl (Fmoc) protecting group and a trifluoromethyl substitution on the tyrosine aromatic ring. As a specialty building block, it is highly valued in peptide chemistry for introducing site-specific fluorinated modifications into peptide sequences. The presence of the trifluoromethyl group imparts distinct electronic and steric properties, making this compound particularly relevant for studies in structure-activity relationships, protein engineering, and the development of novel biomolecular tools. Its integration into synthetic protocols enables researchers to explore the impact of fluorinated residues on peptide conformation, stability, and function, thereby expanding the toolbox available for advanced biochemical investigations.
Peptide Synthesis: N-Fmoc-O-(trifluoromethyl)-L-tyrosine is primarily utilized as a protected amino acid monomer in solid-phase peptide synthesis (SPPS). The Fmoc group allows for selective deprotection under mild basic conditions, facilitating stepwise assembly of peptide chains. Incorporation of the trifluoromethyl-modified tyrosine residue enables the generation of fluorinated peptides, which are valuable for probing the influence of electron-withdrawing substituents on peptide folding, receptor binding, and enzymatic recognition. This application is crucial for the design of peptides with enhanced stability, altered hydrophobicity, or tailored bioactivity.
Structure-Activity Relationship Studies: The unique electronic characteristics conferred by the trifluoromethyl group on the phenolic ring of tyrosine provide a powerful tool for systematic investigation of side-chain modifications in peptide and protein contexts. Researchers employ this derivative to substitute native tyrosine residues and assess the resulting effects on biological activity, binding affinity, and molecular recognition. Such studies are essential for elucidating the contributions of aromatic side chains to protein-protein interactions, enzyme catalysis, and signal transduction mechanisms.
Biophysical and Spectroscopic Probing: The introduction of a trifluoromethyl group into peptide backbones enables the use of advanced spectroscopic techniques, such as 19F nuclear magnetic resonance (NMR), to study molecular dynamics, folding pathways, and intermolecular contacts. The fluorine atoms serve as sensitive probes due to their distinct NMR signatures and minimal background in biological samples. By incorporating N-Fmoc-O-(trifluoromethyl)-L-tyrosine into peptides, researchers gain access to non-invasive methods for monitoring conformational changes and mapping interaction sites with high specificity and resolution.
Protein Engineering: In the context of protein engineering and design, this fluorinated tyrosine analogue serves as a strategic tool for fine-tuning protein properties. The altered steric and electronic environment introduced by the trifluoromethyl group can modulate protein stability, folding kinetics, and resistance to proteolytic degradation. By site-specifically incorporating this residue into engineered proteins or peptide scaffolds, scientists can systematically evaluate the impact of fluorinated side chains on overall molecular behavior and functionality.
Analytical Method Development: The distinct physicochemical properties of the trifluoromethyl-substituted tyrosine residue make it a valuable internal standard or marker for analytical method development in peptide research. Its incorporation into synthetic standards or reference peptides supports the optimization of chromatographic separation, mass spectrometric detection, and quantitative analysis of complex peptide mixtures. This application is particularly relevant for laboratories seeking to improve sensitivity and selectivity in the characterization of fluorinated biomolecules or to validate analytical protocols for peptide-based studies.
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