N-Fmoc-7-methoxy-L-tryptophan features indole O-methylation, altering absorption and stacking behavior. The modification influences peptide fluorescence and aromatic interactions. Researchers employ it in solvent-structure correlation and conformational mapping. Its protected form is compatible with standard solid-phase chemistries.
CAT No: R2109
CAS No:2416720-26-6
Synonyms/Alias:N-Fmoc-7-methoxy-L-tryptophan;2416720-26-6;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(7-methoxy-1H-indol-3-yl)propanoic acid;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(7-methoxy-1H-indol-3-yl)propanoic acid;(S)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-3-(7-methoxy-1H-indol-3-yl)propanoic acid;
N-Fmoc-7-methoxy-L-tryptophan is a chemically protected, non-canonical amino acid derivative widely utilized in modern peptide synthesis and biochemical research. Featuring an N-terminal fluorenylmethyloxycarbonyl (Fmoc) protecting group and a methoxy substitution at the 7-position of the indole ring, this compound offers enhanced utility for the incorporation of modified tryptophan residues into peptide sequences. Its unique structure enables precise modulation of peptide properties, making it a valuable reagent for the exploration of structure-activity relationships, protein engineering, and the development of novel biomolecules. The introduction of the methoxy group imparts distinct electronic and steric characteristics, expanding the toolkit available to researchers seeking to investigate the roles of tryptophan analogues in biological systems.
Peptide Synthesis: N-Fmoc-7-methoxy-L-tryptophan is primarily employed as a building block in solid-phase peptide synthesis (SPPS) and related solution-phase protocols. The Fmoc group provides orthogonal protection, facilitating stepwise assembly of peptides while preserving the integrity of sensitive side chains. Incorporation of this methoxy-substituted tryptophan derivative allows for the generation of peptides with altered electronic environments and steric profiles at the indole moiety, enabling systematic studies of sequence-function relationships and the creation of peptides with tailored properties for biochemical assays.
Structure-Activity Relationship Studies: The methoxy modification at the 7-position of the indole ring introduces subtle changes in hydrogen bonding potential and aromaticity, providing researchers with a tool to probe the functional significance of tryptophan residues in bioactive peptides and proteins. By substituting canonical tryptophan with this analogue, investigators can dissect the contributions of indole ring electronics to receptor binding, enzymatic activity, and protein-protein interactions. This approach is especially valuable in the design of peptidomimetics, receptor ligands, and enzyme substrates where fine-tuning of molecular recognition is required.
Protein Engineering: In the context of protein engineering and synthetic biology, the availability of N-Fmoc-7-methoxy-L-tryptophan enables the site-specific incorporation of non-natural amino acids into recombinant proteins. This strategy supports the development of proteins with enhanced stability, altered fluorescence, or modified biological activity. The unique photophysical and chemical properties imparted by the methoxy group can be leveraged to investigate folding pathways, monitor conformational changes, or introduce novel functional handles for downstream modification.
Analytical Method Development: The distinctive spectroscopic properties of the 7-methoxy-indole chromophore make this derivative useful in method development for peptide and protein analysis. Its altered UV absorbance and fluorescence characteristics can be exploited in high-performance liquid chromatography (HPLC), mass spectrometry, and fluorescence-based detection techniques, aiding in the identification, quantification, and characterization of peptides containing this modified residue. Such analytical advantages are particularly relevant in the quality control and characterization of synthetic peptide libraries.
Biophysical and Mechanistic Studies: The incorporation of 7-methoxy-L-tryptophan into peptides and proteins provides a powerful approach for investigating biophysical properties such as folding, stability, and intermolecular interactions. The methoxy group can modulate the indole ring's electronic distribution, influencing local hydrophobicity and stacking interactions. Researchers utilize this analogue to examine how subtle changes at the tryptophan side chain affect peptide aggregation, membrane association, and conformational dynamics, thereby advancing understanding of protein structure and function at the molecular level.
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