N-Fmoc-3-fluoro-L-tyrosine features a fluorinated phenolic ring that influences hydrogen bonding, dipole orientation, and aromatic character. The modification provides a tool for studying fluorine-driven spectroscopic shifts and residue polarity. Researchers employ it to assess altered peptide folding and solvent effects. Its protected form ensures compatibility with solid-phase methods.
CAT No: R2153
CAS No:1270290-56-6
Synonyms/Alias:1270290-56-6;N-Fmoc-3-fluoro-L-tyrosine;(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(3-fluoro-4-hydroxyphenyl)propanoic acid;(S)-Fmoc-3-Fluoro-Tyrosine;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(3-fluoro-4-hydroxyphenyl)propanoic acid;(2S)-2-{[(9H-FLUOREN-9-YLMETHOXY)CARBONYL]AMINO}-3-(3-FLUORO-4-HYDROXYPHENYL)PROPANOIC ACID;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-3-fluoro-L-tyrosine;SCHEMBL15083325;VNQUEERXNCSBHF-NRFANRHFSA-N;MFCD07783957;AS-84417;CS-0439210;E84615;
N-Fmoc-3-fluoro-L-tyrosine is a specialized amino acid derivative featuring a fluoro substitution at the 3-position of the tyrosine aromatic ring and an N-terminal 9-fluorenylmethoxycarbonyl (Fmoc) protecting group. As a non-canonical amino acid, it combines the structural features of tyrosine with the electronic effects imparted by fluorine, offering unique chemical and biophysical properties. This compound is primarily utilized in peptide synthesis and protein engineering, where site-specific incorporation of fluorinated residues enables sophisticated studies of protein structure, function, and dynamics. Its design allows researchers to probe subtle changes in molecular interactions, enzymatic mechanisms, and conformational behaviors, making it a valuable tool in the fields of chemical biology, medicinal chemistry, and materials science.
Peptide synthesis: N-Fmoc-3-fluoro-L-tyrosine is widely used as a building block in solid-phase peptide synthesis (SPPS), where the Fmoc group serves as a temporary N-terminal protecting group compatible with standard Fmoc/tBu protocols. The incorporation of a fluoro-substituted tyrosine residue into synthetic peptides enables researchers to systematically investigate the effects of aromatic fluorination on peptide stability, folding, and receptor binding. Its use is particularly relevant in the development of modified peptides for structure-activity relationship (SAR) studies and the design of fluorinated peptide analogs with altered physicochemical properties.
Protein engineering: In the context of protein engineering, the introduction of 3-fluoro-L-tyrosine via chemical synthesis or genetic code expansion allows for the exploration of fluorine's influence on protein structure and function. The presence of the fluorine atom can modulate hydrogen bonding, aromatic stacking, and electronic distribution within protein environments, providing insights into the roles of tyrosine residues in catalysis, binding, and stability. Researchers leverage this amino acid analog to dissect subtle energetic contributions and to develop proteins with enhanced or novel functionalities.
Spectroscopic studies: The unique electronic and magnetic properties conferred by the fluorine atom make 3-fluoro-L-tyrosine a valuable probe for spectroscopic investigations. Incorporation of this residue into peptides or proteins facilitates the use of 19F nuclear magnetic resonance (NMR) spectroscopy, enabling site-specific monitoring of conformational changes, ligand interactions, and dynamic processes with high sensitivity and minimal background interference. Such applications are essential for elucidating molecular mechanisms in complex biological systems.
Enzyme mechanism studies: The strategic placement of a fluorine atom on the tyrosine ring can be exploited to investigate enzymatic mechanisms involving tyrosine residues. By substituting native tyrosine with its 3-fluoro analog, researchers can assess the effects of altered electronic properties on enzyme catalysis, substrate recognition, and transition state stabilization. These studies contribute to a deeper understanding of enzyme specificity and the design of mechanism-based inhibitors or probes.
Materials science: Beyond traditional biochemical research, N-Fmoc-3-fluoro-L-tyrosine finds application in the design of novel peptide-based materials. The presence of the fluoro group can influence peptide self-assembly, intermolecular interactions, and material properties such as hydrophobicity and thermal stability. This enables the development of advanced biomaterials, nanostructures, and functional surfaces with tailored characteristics for use in biotechnology and nanotechnology platforms.
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