H-D-HTyr-OH*HBr

H-D-HTyr-OH*HBr is a deuterium-labeled, D-configured tyrosine derivative presented as a hydrobromide salt, featuring a chiral alpha-carbon, a phenolic side chain, and a free carboxylic acid that supports amino-acid coupling chemistry. The tyrosine aromatic ring with a phenolic hydroxyl enables selective derivatization and oxidative or electrophilic substitution strategies while maintaining the stereochemical integrity of the amino-acid backbone. The D-tyrosine stereochemistry and the deuterium label at the alpha position make the molecule suitable for isotopically tracked studies, where mass shifts can be used to monitor incorporation, metabolism, or synthetic transformations. The hydrobromide counterion and salt form influence handling and can assist in maintaining the amino functionality in a protonated state during downstream synthetic steps.

1. Peptide Synthesis

H-D-HTyr-OH*HBr is applied in peptide building workflows where a D-configured tyrosine residue is required for stereodefined peptide coupling and subsequent sequence assembly. The protected amino acid derivative is not indicated here, but the presence of an amino-acid backbone with a carboxylic acid and phenolic side chain supports standard peptide coupling logic after appropriate N-protection and carboxyl activation in the synthetic plan. The phenolic hydroxyl can be managed through protection strategies to prevent side reactions during amide bond formation, enabling controlled incorporation into peptide chains. The deuterium label and D-configuration allow construction of stereochemically defined peptide analogs for mechanistic studies and analytical verification of incorporation.

2. Chemical Biology Labeling

H-D-HTyr-OH*HBr is suited for chemical biology research that relies on isotopic tracing of tyrosine-containing motifs, including studies of peptide uptake, processing, or enzymatic turnover. The deuterium at the alpha position provides a mass-tag handle that can be detected by LC-MS or MS/MS to distinguish labeled intermediates from unlabeled tyrosine derivatives. The phenolic side chain enables conjugation or derivatization routes that can preserve the aromatic recognition element while enabling downstream attachment to biomolecular scaffolds. The hydrobromide salt form supports reproducible handling of the amino acid during derivatization and can be integrated into workflows that generate labeled peptide fragments or protein-modifying reagents.

3. Protein Engineering Studies

H-D-HTyr-OH*HBr can be used as a stereochemically defined tyrosine analog for protein engineering contexts where D-amino-acid incorporation or stereochemical perturbation is used to probe structure-function relationships. The D-configuration at the alpha center and the intact phenolic group allow placement into peptide segments that mimic tyrosine geometry while altering backbone stereochemistry. The carboxylic acid functionality supports conversion into activated forms for incorporation into peptide or protein fragments, while side-chain chemistry can be tuned through phenol protection and later deprotection. The deuterium label can further support residue-level tracking in protein or peptide constructs, enabling analytical differentiation of engineered segments during biochemical characterization.

4. Peptidomimetic Construction

H-D-HTyr-OH*HBr serves as a chiral amino-acid intermediate for peptidomimetic and constrained scaffold synthesis where D-tyrosine stereochemistry influences conformation and binding-site compatibility. The aromatic phenol provides a functional handle for generating electrophilic or nucleophilic derivatives, including routes to ether, ester, or protected phenol intermediates that can be carried into larger scaffold assemblies. The amino-acid backbone can be transformed into coupling-ready intermediates to build amide-linked analogs, supporting iterative synthesis of peptide mimetics with controlled stereocenters. The isotopic deuterium label can be retained into final analogs to enable mechanistic mapping of synthetic incorporation and subsequent stability studies.

5. Analytical Research Standards

H-D-HTyr-OH*HBr is suitable for analytical research and method development where isotopically labeled tyrosine standards are required for quantitation, calibration, or identification of tyrosine-derived species. The combination of D-stereochemistry and deuterium labeling yields a distinctive mass signature, helping distinguish labeled amino acid or labeled peptide fragments from endogenous or unlabeled standards in complex matrices. The phenolic hydroxyl and carboxylic acid features support derivatization strategies that improve chromatographic behavior or enable targeted detection workflows. The hydrobromide salt form can facilitate reproducible preparation of standard solutions and integration into LC-MS/MS or related analytical pipelines for amino-acid and peptide profiling.

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