N-Me-DL-Phe-OMe · HCl

N-Me-DL-Phe-OMe · HCl is a hydrochloride salt of a methylated amino acid ester derived from phenylalanine, featuring a chiral, stereodefinable backbone in the DL (racemic) form and an N-methylated amine that reduces direct peptide-coupling reactivity relative to free amino acids. The structure contains a phenyl side chain for hydrophobic and aromatic interactions, an ester function at the C-terminus (methyl ester) that can be selectively transformed, and a protonated amine as indicated by the HCl salt, which improves handling and enables controlled deprotonation during downstream chemistry. The N-methyl group and ester carbonyl together influence chemoselectivity, making the compound suitable as a protected/activated intermediate for building N-methylated or C-terminally modified peptide fragments. The racemic stereochemistry supports use in synthesis planning where stereochemical purity is not required or where later resolution, stereochemical exchange, or stereochemical screening is part of the workflow.

1. Protected Amino Acid Chemistry

N-Me-DL-Phe-OMe · HCl supports protected amino acid synthesis workflows where N-methylation and esterification define the amine and carboxyl equivalents for controlled derivatization. The N-methylated amine can be managed through salt formation and subsequent deprotonation, while the methyl ester can undergo hydrolysis or transesterification to access carboxylic acid derivatives for further coupling. The phenylalanine-derived aromatic side chain remains chemically stable under many standard peptide-building conditions, enabling downstream functional group compatibility in fragment assembly. Racemic stereochemistry can be applied in preparative routes for screening libraries or for intermediates that later undergo stereochemical adjustment.

2. Peptide Synthesis

N-Me-DL-Phe-OMe · HCl is applicable to peptide synthesis strategies targeting N-methylated phenylalanine residues or C-terminally esterified peptide fragments. The methyl ester at the carboxyl terminus can be converted into a carboxylate for coupling chemistry or retained when ester-capped peptide analogs are desired for stability or conformational studies. The N-methyl substituent enables construction of peptide backbones bearing N-methyl amide motifs, which are commonly used to modulate proteolytic stability and backbone conformation in peptidomimetics. The DL configuration permits use in racemate-based peptide fragment generation and subsequent stereochemical evaluation in structure-activity relationship studies.

3. Peptidomimetics And SAR

N-Me-DL-Phe-OMe · HCl serves chemical biology and medicinal chemistry workflows focused on peptidomimetics and SAR studies where N-methylated amino acid units and aromatic side chains are key scaffold elements. The phenyl group provides a hydrophobic/aromatic interaction handle, while the N-methyl amide pattern can be carried into larger constructs to tune conformational preferences and binding-site mimicry. The ester functionality can be transformed into acids or converted into alternative C-terminal groups, supporting the preparation of analog series with systematic C-terminal modifications. Racemic input can be used for early-stage library synthesis, with later stereochemical resolution or selective incorporation planned when stereochemical effects become a primary variable.

4. Process Chemistry Intermediate

N-Me-DL-Phe-OMe · HCl fits process chemistry intermediate preparation where salt formation, ester handling, and N-methyl amino acid architecture support scalable fine chemical manufacturing routes. The hydrochloride form facilitates storage and controlled deprotonation behavior, while the methyl ester provides a defined carboxyl equivalent for downstream conversion into coupling-ready acids or activated derivatives. The N-methyl substitution and aromatic side chain can be compatible with protecting-group strategies that minimize side reactions during multistep synthesis, including selective hydrolysis or functional group interconversions at the ester. The compound's role as a chiral amino acid intermediate in racemic form aligns with industrial workflows that prioritize robust transformations and subsequent purification or stereochemical tailoring steps.

5. Analytical Standards And Method Development

N-Me-DL-Phe-OMe · HCl can be employed in analytical research and method development as a reference material for amino acid ester and N-methylated amino acid derivative profiling. The combination of an aromatic phenylalanine side chain, a methyl ester, and an N-methylated amine produces characteristic chromatographic and mass spectrometric signatures that can support calibration and identification in complex peptide or metabolite matrices. Hydrolysis and derivatization of the ester function can generate related standards for validating conversion steps, while the HCl salt form helps define ionization behavior for instrumental analysis. Racemic composition can be useful when analytical methods are intended to quantify total stereoisomer content or when stereochemical separation is not required for the measurement objective.

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