H-D-Arg-OMe*2HCl

H-D-Arg-OMe*2HCl is a D-configured arginine methyl ester supplied as a dihydrochloride salt, combining a stereochemically defined amino acid backbone with a protected carboxyl functionality as the O-methyl ester. The molecule contains a guanidinium side chain characteristic of arginine, which is strongly protonated under acidic conditions and can participate in salt formation, hydrogen-bonding networks, and ionic interactions during peptide coupling and downstream derivatization. The D-stereocenter at the α-position provides a chiral, non-proteinogenic configuration that supports stereocontrolled synthesis of D-arginine-containing peptides and peptidomimetics, while the ester form enables conversion to activated carboxyl equivalents or controlled hydrolysis to regenerate the free acid. The dihydrochloride counterions increase handling stability and solubility in polar media, making the compound suitable as a chiral amino acid ester intermediate for peptide building block preparation and biochemical research workflows.

1. Protected Amino Acid Chemistry

H-D-Arg-OMe*2HCl is used in protected amino acid synthesis workflows where the methyl ester and guanidinium functionality must be managed orthogonally during coupling chemistry. The O-methyl ester can be transformed into carboxyl-activated derivatives for peptide bond formation, while the protonated guanidinium can be temporarily stabilized as a salt to maintain reactivity control during intermediate handling. D-configuration at the α-carbon enables stereochemically defined incorporation into peptide sequences that require non-natural stereochemistry for stability or mechanistic studies. Downstream conversion to D-arginine-based building blocks supports iterative assembly of protected amino acid intermediates used in fine chemical synthesis and peptide manufacturing development.

2. Peptide Synthesis

H-D-Arg-OMe*2HCl serves as a D-arginine methyl ester input for peptide synthesis strategies that require compatibility with standard amide-forming coupling conditions. The arginine guanidinium side chain provides a strongly basic functionality that can be carried through as a salt form or selectively protected in broader synthetic schemes to reduce side reactions during chain assembly. The ester handle supports controlled generation of the C-terminal functionality for coupling or for subsequent hydrolysis to the free acid when designing C-terminal modified peptides. D-stereochemistry enables construction of D-Arg-containing peptides and peptidomimetic scaffolds for structure-activity relationship studies and stereochemical mapping of peptide recognition.

3. Bioconjugation Chemistry

H-D-Arg-OMe*2HCl can be applied to bioconjugation and chemical biology workflows that rely on arginine's cationic guanidinium for electrostatic association and linker design. The methyl ester and amino functionality can be leveraged as a synthetic intermediate toward amide or carbamate linkers, enabling attachment of D-arginine residues to carriers, probes, or biomolecular scaffolds. The D-configuration supports incorporation of stereodefined residues that may alter protease susceptibility and influence labeling stability in experimental reagent preparation. Guanidinium-driven binding motifs can be used to construct conjugates for biomolecule modification, affinity-based capture, and analytical probe generation within applied research and industrial laboratory supply chains.

4. Peptidomimetics And SAR Studies

H-D-Arg-OMe*2HCl is suitable for peptidomimetic construction where D-arginine stereochemistry and the guanidinium side chain are used to tune molecular recognition. The side-chain guanidinium provides a persistent hydrogen-bonding and ionic interaction pattern that can be preserved while the backbone stereochemistry is inverted relative to proteinogenic L-arginine. The ester form supports synthetic diversification into C-terminal variants, including conversion to free acid for further derivatization or activation for scaffold assembly. Downstream analog libraries prepared from this chiral amino acid intermediate can support SAR studies focused on stereochemical effects, binding mode hypotheses, and structure-function relationships in peptide-like systems.

5. Process Chemistry Intermediate

H-D-Arg-OMe*2HCl is relevant to process chemistry intermediate preparation for manufacturing routes that require a stable, isolable chiral amino acid ester salt. The dihydrochloride salt form improves handling characteristics in polar processing steps, while the methyl ester provides a controllable carboxyl equivalent for conversion to activated intermediates or for regulated hydrolysis during scale-up. The D-arginine stereocenter supports reproducible stereochemical outcomes in industrial fine chemical synthesis where stereochemical integrity is required for downstream peptide building block consistency. The compound's functional group set enables integration into broader manufacturing sequences for protected amino acid derivatives and peptide-grade intermediates used in specialty chemical production.

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