N-Fmoc-O-methyl-3-chloro-L-tyrosine is a halogenated tyrosine analog featuring O-methyl protection and aromatic chlorination. These modifications alter polarity, steric hindrance, and hydrogen-bonding potential. Researchers use it to study aromatic interactions, enzyme recognition, and modified spectroscopic profiles. Its protecting groups enhance synthetic manageability.
CAT No: R2144
CAS No:2002503-89-9
Synonyms/Alias:N-Fmoc-O-methyl-3-chloro-L-tyrosine;2002503-89-9;(2S)-3-(3-chloro-4-methoxyphenyl)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}propanoic acid;F81107;(2S)-3-(3-chloro-4-methoxyphenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)propanoic acid;
N-Fmoc-O-methyl-3-chloro-L-tyrosine is a specialized amino acid derivative designed for advanced peptide synthesis and biochemical research applications. Featuring a fluorenylmethyloxycarbonyl (Fmoc) protecting group on the amino terminus, an O-methyl modification on the phenolic hydroxyl, and a chlorine substituent at the 3-position of the aromatic ring, this compound enables precise manipulation of peptide sequences and side-chain functionalities. Its unique structure allows researchers to introduce both steric and electronic diversity into synthetic peptides, facilitating the exploration of structure-activity relationships and the development of novel biomolecules. As a non-canonical tyrosine analog, it supports the creation of peptides with enhanced stability, altered reactivity, and tailored biophysical properties, making it a valuable tool in modern peptide chemistry and protein engineering.
Peptide synthesis: N-Fmoc-O-methyl-3-chloro-L-tyrosine is widely employed as a building block in solid-phase peptide synthesis (SPPS). The Fmoc protection ensures compatibility with standard Fmoc/tBu peptide assembly protocols, while the O-methyl group prevents undesired side reactions at the phenolic oxygen during chain elongation. The 3-chloro substitution further expands the chemical diversity accessible in synthetic peptides, enabling the systematic investigation of the effects of halogenation on peptide conformation, stability, and biological recognition. By facilitating the incorporation of this modified residue into defined positions within peptide sequences, researchers can generate peptides with unique physicochemical and functional attributes.
Structure-activity relationship studies: The incorporation of O-methyl and 3-chloro modifications into tyrosine residues provides a powerful approach for probing the influence of side-chain electronic and steric alterations on peptide and protein behavior. By substituting canonical tyrosine with this derivative, scientists can dissect the roles of hydrogen bonding, aromaticity, and halogen interactions in modulating binding affinities, enzymatic activity, and molecular recognition. Such studies are critical for mapping functional hotspots in bioactive peptides, optimizing ligand-receptor interactions, and guiding the rational design of new therapeutics and molecular probes.
Peptide-based probe development: The unique chemical features of this tyrosine analog make it suitable for the design of specialized peptide probes and molecular tools. The O-methylation imparts increased resistance to enzymatic oxidation and phosphorylation, while the 3-chloro group can serve as a spectroscopic or chemical handle for further modification. These properties enable the generation of stable, site-specifically labeled peptides for use in biophysical assays, target identification, and mechanistic studies. Researchers can leverage these attributes to develop probes that retain native-like recognition while exhibiting enhanced durability in complex biological environments.
Combinatorial library synthesis: N-Fmoc-O-methyl-3-chloro-L-tyrosine is valuable in the construction of combinatorial peptide libraries aimed at high-throughput screening and lead discovery. Its incorporation expands the chemical space explored within libraries, allowing for the identification of novel peptide sequences with improved binding or functional properties. The presence of the O-methyl and chloro modifications can modulate peptide folding, solubility, and target specificity, thereby increasing the likelihood of discovering candidates with desirable biophysical and pharmacological profiles. This approach accelerates the development of next-generation peptide-based materials and molecular scaffolds.
Protein engineering and biomaterials research: The strategic introduction of modified tyrosine residues into synthetic proteins and biomaterials enables the fine-tuning of their structural and functional characteristics. By replacing native tyrosine with the O-methyl-3-chloro analog, researchers can engineer proteins with altered reactivity, enhanced stability, or novel chemical reactivity at designated sites. Such modifications are instrumental in the design of protein-based materials with tailored properties, the creation of site-specific conjugates, and the study of non-canonical amino acid incorporation in protein biosynthesis. These applications support the advancement of synthetic biology, materials science, and bioengineering initiatives.
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