H-Met(O)-OH

H-Met(O)-OH is a methionine-derived amino acid bearing a hydroxylated sulfur functionality, formulated as the free amino acid with an N-terminal hydrogen and a carboxylic acid group. The side chain contains a stereochemically defined sulfur center in the methionine sulfoxide motif, introducing polarity and distinct oxidation-state reactivity compared with unmodified methionine. The molecule features an amino group and a carboxylic acid that can participate in peptide coupling chemistry, while the sulfoxide-like oxygenated sulfur can influence coordination behavior, oxidation/reduction susceptibility, and chemical stability under coupling and purification conditions. As a chiral amino acid intermediate, H-Met(O)-OH can serve as a chemically defined building block for constructing sulfur-oxidation-state sensitive peptides and for downstream derivatization where controlled stereochemistry at sulfur is required.

1. Peptide Synthesis

H-Met(O)-OH is applied in peptide building block preparation where amino acid coupling to form amide bonds is required, leveraging its free amino functionality and carboxylic acid for standard peptide coupling logic. The hydroxylated sulfur side chain can be preserved under appropriately chosen coupling and workup conditions, enabling incorporation of a methionine-oxidation-state motif into peptide sequences for chemical biology and materials research. N- and C-terminal reactivity can be managed through temporary protection strategies during synthesis, followed by deprotection to yield defined peptide termini. Downstream peptide analogs prepared from H-Met(O)-OH can be used to probe how sulfur oxidation state affects peptide conformation, stability, and chemical reactivity in synthetic and analytical workflows.

2. Chemical Biology

H-Met(O)-OH supports chemical biology research focused on oxidation-state controlled labeling and redox-sensitive molecular recognition, where the oxygenated sulfur side chain provides a distinct physicochemical handle relative to methionine. The amino and carboxyl groups enable conjugation to carrier proteins, linkers, or solid supports after conversion to activated derivatives, while the sulfur oxygenated functionality can participate in selective transformations or serve as a stereochemical marker. Incorporation into peptide probes can be used to generate defined substrates for studying oxidation-dependent binding events and to create molecular standards for monitoring sulfur-state transitions. H-Met(O)-OH therefore functions as a chemically defined intermediate for constructing oxidation-aware biomolecular tools and for mapping structure-reactivity relationships in amino acid chemistry.

3. Protein Engineering

H-Met(O)-OH is suitable for protein engineering workflows that require chemically synthesized peptides or protein fragments containing a methionine oxidation-state element, particularly when site-specific chemical incorporation is preferred over genetic encoding. The chiral sulfur-containing side chain can be retained as a stereochemically informative feature within engineered sequences, while the amino acid backbone enables assembly into longer constructs through peptide ligation-compatible strategies. Temporary protection of the amino and carboxyl functionalities can be used to control coupling order and to generate fragments for fragment condensation or conjugation to biomolecular scaffolds. Resulting engineered peptide segments can serve as substrates or reference materials for examining how sulfur oxidation state influences local structure, proteolytic susceptibility, or chemical stability in protein-mimetic systems.

4. Peptidomimetics

H-Met(O)-OH is used in peptidomimetic construction where the hydroxylated sulfur side chain acts as a targeted functional element for tuning polarity, hydrogen-bonding patterns, and oxidation-state dependent behavior. The free amino acid framework can be transformed into protected derivatives for stepwise assembly of constrained analogs, including incorporation into cyclic or sterically constrained peptide-like scaffolds. The stereochemical sulfur element can be maintained to reproduce oxidation-state-specific interactions in SAR studies and molecular design programs. Peptidomimetics derived from H-Met(O)-OH can be applied as chemical probes, scaffold components, or reference standards for evaluating how sulfur oxidation state modulates binding-relevant properties.

5. Analytical Standards

H-Met(O)-OH is employed as an analytical research intermediate and reference material for quantifying methionine oxidation-state species and for method development in amino acid and peptide analysis. The combination of amino acid functionality and oxygenated sulfur enables derivatization to detectable forms, generation of calibration standards, or preparation of internal standards after conversion to protected or activated analogs. The stereochemical sulfur motif supports discrimination of oxidation-state-specific peaks in chromatographic and mass spectrometric workflows when paired with appropriate derivatization chemistry. H-Met(O)-OH thus serves as a chemically defined anchor for analytical method validation and for monitoring oxidation-related transformations in peptide and protein sample matrices.

6. Process Chemistry Intermediate

H-Met(O)-OH can be applied as a chiral amino acid intermediate in process chemistry and fine chemical synthesis where controlled sulfur oxidation-state incorporation is required for downstream manufacturing of peptide building blocks or functionalized amino acid derivatives. The presence of both amino and carboxylic acid groups supports conversion into activated intermediates for coupling steps, while the oxygenated sulfur side chain provides a defined functional group that can be carried through multi-step sequences with stereochemical tracking. Protection-group strategies for the amino and carboxyl functions can be integrated into manufacturing routes to manage chemoselectivity during peptide coupling or derivatization. Industrially, H-Met(O)-OH-derived intermediates can feed into specialty chemical production of sulfur-oxidation-state specific peptides, peptidomimetics, and analytical reference materials used across biochemical research and applied chemical development.

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