N-Fmoc-6-fluoro-L-tryptophan contains a fluorinated indole ring that modulates electronic distribution and hydrogen-bonding capacity. Researchers use it to analyze altered π-electron density and probe solvent interactions. The residue enhances spectroscopic versatility in structural studies. Its protection supports synthetic incorporation.
CAT No: R2110
CAS No:908847-01-8
Synonyms/Alias:N-Fmoc-6-fluoro-L-tryptophan;908847-01-8;Fmoc-6-fluoro-L-tryptophan;Fmoc-Trp(6-F)-OH;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(6-fluoro-1H-indol-3-yl)propanoic acid;(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(6-fluoro-1H-indol-3-yl)propanoic acid;Fmoc-6-F-Trp-OH;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(6-fluoro-1H-indol-3-yl)propanoic acid;MFCD29917530;DTXSID501194033;AT34076;FF79053;BS-45591;N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-6-fluoro-L-tryptophan;(S)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-(6-fluoro-1H-indol-3-yl)propanoicacid;
N-Fmoc-6-fluoro-L-tryptophan is a protected, fluorinated derivative of the canonical amino acid L-tryptophan, featuring both a 9-fluorenylmethyloxycarbonyl (Fmoc) protecting group and a fluorine atom substitution at the 6-position of the indole ring. The compound is primarily utilized in the context of solid-phase peptide synthesis (SPPS), where the Fmoc group enables orthogonal protection strategies, and the fluorinated residue introduces unique physicochemical and spectroscopic properties into peptide sequences. Its dual modification makes it of particular interest to researchers exploring the structure-activity relationships of peptides, as well as those investigating the impact of fluorinated amino acids on protein function, stability, and molecular recognition.
Peptide Synthesis: N-Fmoc-6-fluoro-L-tryptophan is widely employed as a building block in Fmoc-based solid-phase peptide synthesis. The Fmoc group provides temporary N-terminal protection, allowing for stepwise assembly of peptide chains under mild deprotection conditions that preserve the integrity of sensitive side chains. Incorporation of the 6-fluoro substituent into peptide sequences enables the generation of analogs with altered electronic and steric profiles, facilitating the study of fluorine's effects on peptide folding, receptor binding, and overall bioactivity. The compound's compatibility with standard SPPS protocols ensures its utility for both small-scale research and larger preparative syntheses.
Structure-Activity Relationship Studies: The introduction of a fluorine atom at the 6-position of the indole ring in tryptophan offers a powerful tool for probing the role of aromatic residues in peptide and protein function. By substituting canonical tryptophan with this fluorinated analog, researchers can systematically investigate changes in hydrogen bonding, π-π stacking, and hydrophobic interactions within peptide frameworks. Such studies are instrumental in mapping critical interaction sites, optimizing ligand-receptor affinity, and designing peptides with enhanced selectivity or stability.
Protein Engineering: In the field of protein engineering, 6-fluoro-L-tryptophan derivatives are incorporated into proteins to modulate their physical and chemical properties. The electron-withdrawing effects of the fluorine atom can influence the local environment of the indole ring, affecting protein folding dynamics and stability. These modifications are particularly valuable in the rational design of proteins with improved resistance to proteolysis or altered spectroscopic signatures, supporting applications in biochemical research and the development of novel biomaterials.
Spectroscopic Probes: The presence of a fluorine atom in the indole moiety provides a distinct advantage for spectroscopic investigations. 6-fluoro-substituted tryptophan residues serve as sensitive probes in 19F NMR and fluorescence spectroscopy, offering site-specific information on local environments, conformational changes, and molecular interactions within peptides and proteins. The unique spectroscopic properties of the fluorinated residue can be harnessed to monitor folding, binding events, or dynamic processes in real time, making it a valuable tool for advanced biophysical studies.
Analytical Method Development: The use of N-Fmoc-6-fluoro-L-tryptophan as a standard or reference compound aids in the development and validation of analytical techniques for fluorinated amino acids and peptides. Its well-defined chemical structure and distinctive fluorine signature facilitate method optimization in high-performance liquid chromatography (HPLC), mass spectrometry, and NMR-based assays. Such applications are essential for ensuring accurate quantification, purity assessment, and structural verification of fluorinated biomolecules in research and industrial settings.
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