N-Fmoc-3-methyl-L-tyrosine is a methylated tyrosine analog featuring altered aromatic electronics and steric influence. The modification affects hydrogen bonding and conformational bias. Researchers use it to tune peptide stability, aromatic interactions, and spectroscopic properties. Its Fmoc protection enables seamless synthetic incorporation.
CAT No: R2140
CAS No:1145678-51-8
Synonyms/Alias:N-Fmoc-3-methyl-L-tyrosine;1145678-51-8;Fmoc-L-Tyr(3-Me)-OH;(2S)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}-3-(4-hydroxy-3-methylphenyl)propanoic acid;(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-(4-hydroxy-3-methylphenyl)propanoic acid;MFCD30749167;CS-0212782;E70929;
N-Fmoc-3-methyl-L-tyrosine is a synthetic amino acid derivative featuring an N-terminal fluorenylmethyloxycarbonyl (Fmoc) protecting group and a methyl substitution at the 3-position of the tyrosine aromatic ring. As a specialized building block, it is widely employed in the field of peptide chemistry, particularly for the solid-phase synthesis of custom peptides incorporating non-canonical residues. The Fmoc group allows for efficient stepwise elongation of peptide chains while preserving the integrity of the amino acid side chain, and the methyl modification introduces unique steric and electronic properties. These attributes make the compound a valuable tool for researchers investigating structure-activity relationships, protein engineering, and the development of bioactive peptides with enhanced or novel functionalities.
Peptide synthesis: N-Fmoc-3-methyl-L-tyrosine is primarily utilized as a protected amino acid monomer in Fmoc-based solid-phase peptide synthesis (SPPS). The Fmoc group provides orthogonal protection, enabling selective deprotection and coupling cycles essential for the assembly of complex peptide sequences. The presence of the 3-methyl group on the tyrosine side chain introduces steric hindrance and electronic modulation, which can be strategically employed to influence peptide folding, stability, or resistance to enzymatic degradation. This makes the compound particularly useful in the synthesis of peptides designed to probe the effects of side-chain modifications on biological activity or molecular recognition.
Structure-activity relationship studies: Incorporation of 3-methyl-L-tyrosine into peptide sequences facilitates the systematic evaluation of how subtle side-chain alterations affect peptide-receptor interactions, binding affinity, or functional selectivity. By substituting canonical tyrosine residues with its methylated analogue, researchers can dissect the roles of steric bulk and electronic characteristics in modulating protein-ligand interactions. This approach is instrumental in the rational design of peptide-based inhibitors, agonists, or molecular probes for biochemical and pharmacological investigations.
Protein engineering and design: The use of N-Fmoc-3-methyl-L-tyrosine expands the chemical diversity accessible in engineered proteins and peptides. Its incorporation enables the generation of variants with altered physicochemical properties, such as modified hydrophobicity or aromatic stacking potential. These features are advantageous for tuning protein folding, stability, or intermolecular interactions in synthetic biology projects and biophysical studies. The compound supports the creation of novel peptide scaffolds or protein mimetics with tailored functionalities.
Analytical method development: Modified amino acids like 3-methyl-L-tyrosine serve as valuable standards or reference compounds in analytical chemistry. Their unique mass and chromatographic properties assist in the calibration and validation of analytical techniques, including high-performance liquid chromatography (HPLC) and mass spectrometry (MS). This application is particularly relevant for laboratories developing or optimizing methods for peptide mapping, impurity profiling, or the detection of post-translational modifications.
Biophysical and conformational studies: The introduction of a methyl group at the 3-position of tyrosine provides a means to probe the influence of side-chain modifications on peptide secondary structure and dynamics. By incorporating this derivative into model peptides, researchers can investigate how local changes in steric environment affect backbone conformation, hydrogen bonding, or aromatic interactions. These studies contribute to a deeper understanding of protein folding mechanisms and the design of peptides with desired structural properties.
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