H-D-MePhe-OH*HCl

H-D-MePhe-OH*HCl is the hydrochloride salt of an N-unprotected, α-amino acid derivative featuring a deuterated methyl-substituted phenylalanine motif (MePhe) and a free carboxylic acid, with stereochemical identity preserved at the amino acid α-center as indicated by the deuterated label. The structure combines an aniline-like aromatic ring with a benzylic side chain and a deuterium-containing substituent that can be leveraged for kinetic, metabolic, or mechanistic studies while maintaining peptide-compatible amino acid reactivity. Salt formation with HCl increases aqueous handling of the amino group and supports controlled coupling chemistry under standard peptide synthesis conditions. The presence of both a primary amino functionality and a carboxylic acid enables straightforward conversion into protected amino acid derivatives, peptide building blocks, and downstream analytical or synthetic intermediates.

1. Peptide Synthesis

H-D-MePhe-OH*HCl is used in peptide building block preparation for solid-phase or solution-phase peptide synthesis where a deuterated phenylalanine analog is required for labeled peptide construction. The free amino group and carboxylate functionality can be orthogonally protected (commonly as an N-protecting group and, when needed, as a temporary carboxyl activation handle) to support amide bond formation with carboxylic acids or activated esters from other amino acid residues. The aromatic side chain participates in typical coupling and purification workflows for peptidic scaffolds, while the deuterium label enables mass-tagged peptide sequences for tracing, MS quantitation, or mechanistic comparisons. Incorporation into peptide chains supports generation of deuterated analogs for peptide science and peptidomimetic development, including studies where isotopic substitution affects fragmentation patterns or kinetic isotope effects.

2. Chemical Biology Labeling

H-D-MePhe-OH*HCl serves as an amino acid labeling reagent for chemical biology workflows that require deuterium incorporation into proteinogenic frameworks. The α-amino acid backbone allows conversion into protected derivatives that can be incorporated into peptides or used for controlled derivatization prior to conjugation to biomolecular targets. The deuterated methyl-phenylalanine side chain can be exploited to distinguish labeled species in LC-MS/MS, to monitor incorporation efficiency in synthetic libraries, or to probe labeling-dependent changes in binding or processing without altering the overall aromatic recognition element. Downstream use commonly includes preparation of labeled peptide probes, internal standards, and mechanistic comparison reagents for amino acid incorporation and peptide processing studies.

3. Chiral Amino Acid Intermediate

H-D-MePhe-OH*HCl is applied as a chiral amino acid intermediate for stereochemically defined synthetic routes that require retention of configuration at the α-center. The compound's free carboxylic acid and amino salt form facilitate conversion into activated intermediates for subsequent transformations, including esterification, amide formation, or preparation of N-protected amino acid derivatives used in chiral synthesis planning. The deuterium-containing substituent provides a controlled isotopic handle that can be carried through multi-step sequences to produce labeled chiral intermediates for mechanistic studies or isotopically edited SAR workflows. The resulting protected or activated derivatives can serve as inputs for peptide coupling chemistry, side-chain functionalization sequences, and downstream fine chemical synthesis where stereochemical fidelity and isotopic integrity are required.

4. Analytical Research Standards

H-D-MePhe-OH*HCl is utilized to prepare deuterium-containing analytical standards for amino acid and peptide quantitation by mass spectrometry and related chromatographic methods. The defined amino acid structure, including the aromatic side chain and α-carboxylic acid, supports conversion into reference peptides or derivatized forms that improve chromatographic behavior and enable consistent ionization characteristics. The deuterium label helps resolve analyte and isotopologue peaks, supporting accurate isotope-dilution strategies and improved confidence in peptide identification workflows. Downstream applications include internal standards for metabolite profiling of amino acid analogs, calibration reagents for labeled peptide assays, and reference materials for method development in biochemical research and industrial quality monitoring.

5. Pharmaceutical Intermediate Preparation

H-D-MePhe-OH*HCl is suitable for pharmaceutical intermediate preparation where isotopically labeled amino acid building blocks are required for process development, analytical method validation, or deuterated impurity profiling. The amino acid salt form supports controlled derivatization into N-protected amino acid derivatives and activated carboxyl derivatives that are compatible with peptide coupling steps used to construct deuterated drug-like scaffolds or peptide-based intermediates. The aromatic side chain and carboxylic acid functionality allow integration into synthetic sequences that generate defined residues for peptidomimetic construction, including C-terminal or side-chain-modified intermediates. The deuterium label can be carried into downstream synthetic targets to enable traceability of intermediates, impurity mapping, and robust analytical characterization during specialty chemical production and process chemistry development.

6. Side-Chain Functionalization

H-D-MePhe-OH*HCl can be employed for side-chain functionalization strategies that begin from a deuterated phenylalanine framework and proceed through protection-controlled chemistry. The aromatic ring and benzylic side chain enable downstream transformations that may introduce substituents for conjugation handles, steric tuning, or altered physicochemical properties while maintaining the α-amino acid core for subsequent peptide coupling. The deuterium label provides a stable isotopic marker through derivatization, supporting mechanistic comparisons between functionalized analogs and unlabeled counterparts. Resulting functionalized amino acid derivatives can feed into peptide analog construction, bioconjugation chemistry, and synthetic methodology development where labeled side-chain variants are required for structure-function studies.

1. Odorant binding protein based biomimetic sensors for detection of alcohols associated with Salmonella contamination in packaged beef

2. P-selectin and Complement’s Role in a Neonatal Model of Germinal Matrix Hemorrhage-Induced Secondary Injury

3. Quantitative Analysis of Ligands Effects on Bioefficacy of Nanoemulsion encapsulating Depigmenting Active

4. An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I

5. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle