H-L-Met-OMe*HCl

H-L-Met-OMe*HCl is a methionine methyl ester hydrochloride presented as the L-amino acid methyl ester salt, featuring the L-configuration at the α-carbon and a side chain containing a thioether (-S-CH3) that can participate in nucleophilic and oxidation-state-dependent transformations. The esterified carboxyl group and protonated amine (as the HCl salt) create a controlled reactivity profile that supports peptide coupling chemistry after appropriate activation or salt management. The thioether side chain provides a chemically distinct handle for selective derivatization, including conversion to sulfoxide/sulfone analogs or functional group interconversions used in amino acid modification studies. As a chiral amino acid ester, H-L-Met-OMe*HCl functions as a practical intermediate for building protected amino acid derivatives and for preparing downstream peptide building blocks and analytical standards.

1. Peptide Coupling Chemistry

H-L-Met-OMe*HCl is employed in peptide synthesis workflows where an amino acid ester is required as a protected or temporary carboxyl surrogate during fragment assembly. The L-methionine backbone provides an α-amino group and a stereodefined chiral center, while the methyl ester can be activated for coupling or later converted to carboxylic acid derivatives for amide bond formation. Salt formation with HCl helps manage amine protonation during handling, enabling compatibility with standard peptide coupling strategies after base-mediated neutralization. The thioether side chain remains chemically addressable for orthogonal functionalization, supporting the preparation of methionine-containing peptide segments and peptide analogs for structure-focused studies.

2. Side-Chain Functionalization

H-L-Met-OMe*HCl is suitable for side-chain functionalization programs that use methionine's thioether as a tunable chemical motif. The sulfur atom in the thioether can undergo controlled oxidation to sulfoxide or sulfone forms, enabling stereochemical and electronic modulation of sulfur-containing amino acid derivatives. The methyl ester and protonated amine allow the compound to be carried through derivatization sequences as a chiral intermediate, with downstream hydrolysis or conversion to acid forms to enable incorporation into peptides or conjugates. Resulting methionine sulfur-oxidation analogs can serve as mechanistic probes in chemical biology and as building blocks for peptidomimetic construction where sulfur redox state is a design variable.

3. Protected Amino Acid Intermediate

H-L-Met-OMe*HCl is used as a chiral amino acid intermediate for manufacturing protected methionine derivatives that are compatible with automated peptide synthesis and orthogonal deprotection schemes. The presence of the α-amino functionality and the esterified carboxyl group supports conversion into N-protected amino acids and activated carboxylic acid equivalents through standard protection and ester-to-acid transformations. The L-stereochemistry is retained through these intermediate steps, which is essential for consistent peptide stereochemical outcomes and reproducible coupling behavior. The methionine thioether side chain can be maintained or selectively protected/modified depending on the intended peptide context, enabling reliable downstream assembly of methionine-containing sequences and related synthetic intermediates.

4. Chemical Biology Probes

H-L-Met-OMe*HCl can be applied in chemical biology research to generate methionine-based probes that interrogate sulfur-dependent recognition, redox chemistry, or site-specific modification patterns. The thioether side chain provides a functional handle for derivatization into oxidized sulfur analogs or for conjugation strategies that depend on controlled sulfur reactivity. The amino acid methyl ester form supports incorporation into larger molecular scaffolds, including peptide fragments and labeled amino acid derivatives, where the α-chiral center contributes to stereospecific interactions. Downstream products derived from H-L-Met-OMe*HCl can be used as reference materials, substrate analogs, or structural components in studies of amino acid reactivity and biomolecular modification chemistry.

5. Pharmaceutical Intermediate Preparation

H-L-Met-OMe*HCl is relevant to pharmaceutical intermediate preparation where methionine methyl ester salts serve as feedstocks for synthesizing amino acid derivatives used in active ingredient scaffolds and peptide-like intermediates. The combination of a defined L-amino acid stereocenter, a carboxyl ester handle, and a thioether side chain enables conversion into carboxylic acid forms, N-protected derivatives, and sulfur-modified analogs used in process chemistry. The salt form supports practical handling and can be integrated into manufacturing routes that require controlled amine protonation states prior to protection or activation steps. Methionine-derived intermediates prepared from H-L-Met-OMe*HCl can then be directed toward fine chemical synthesis of peptide building blocks, peptidomimetic motifs, and other amino acid-derived components used in applied chemical manufacturing.

1. Application of human liver organoids as a patient-derived primary model for HBV infection and related hepatocellular carcinoma

2. Olfactory receptor based piezoelectric biosensors for detection of alcohols related to food safety applications

3. Constitutive and inflammation-dependent antimicrobial peptides produced by epithelium are differentially processed and inactivated by the commensal Finegoldia magna and the pathogen Streptococcus pyogenes

4. Relatedness of antibodies to peptides containing homocitrulline or citrulline in patients with rheumatoid arthritis

5. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die