H-alpha-Me-D-Tyr-OH

H-alpha-Me-D-Tyr-OH is a D-configured tyrosine derivative bearing an alpha-methyl substituent at the stereogenic center adjacent to the amino acid backbone, with a free carboxylic acid and a phenolic side chain characteristic of Tyr chemistry. The molecule's aromatic phenol enables selective derivatization through O-alkylation, O-acylation, or oxidative transformations, while the alpha-methyl substitution can influence conformational preference and peptide backbone geometry during coupling. The free amino acid functionality supports standard peptide coupling workflows after appropriate temporary protection of the amino group, and the D stereochemistry provides a practical handle for stereochemical control in unnatural amino acid incorporation. As a chiral amino acid intermediate, H-alpha-Me-D-Tyr-OH can be used to access downstream protected amino acid derivatives, side-chain functional analogs, and stereodefined peptide or peptidomimetic structures.

1. Peptide Synthesis

H-alpha-Me-D-Tyr-OH serves as a stereodefined peptide building block precursor for solid-phase or solution-phase peptide coupling strategies targeting D-amino acid incorporation. The free carboxylic acid and the tyrosine phenol allow conversion into an N-protected, O-protected form suitable for amide bond formation, where the alpha-methyl group can modulate steric approach and backbone conformations in the growing chain. D stereochemistry supports the construction of peptides with defined stereochemical patterns for mechanistic studies, protease resistance evaluation, and backbone-constraint design. Downstream protected derivatives enable sequential coupling at the amino acid level and facilitate C-terminal or internal residue placement in peptide analog libraries for chemical biology research.

2. Peptidomimetics And SAR Studies

H-alpha-Me-D-Tyr-OH is applicable to peptidomimetic construction where alpha-methylation and D-configuration are used to tune local conformation around the tyrosine side chain. The phenolic functionality supports attachment of linkers, fluorophores, or electrophilic handles after controlled O-functionalization, while the alpha-methyl stereocenter can be leveraged to generate structure-activity relationship (SAR) series with systematic stereochemical variation. Incorporation of this chiral amino acid analog into constrained scaffolds can support mapping of binding-site tolerance for backbone substitution and side-chain reactivity. The resulting stereodefined intermediates can be advanced into fragment-based SAR workflows and medicinal chemistry programs focused on non-natural residue effects.

3. Chemical Biology Labeling

H-alpha-Me-D-Tyr-OH can be employed in chemical biology workflows requiring tyrosine-derived conjugation chemistry with defined stereochemistry. The phenolic oxygen can be derivatized to introduce reactive esters, carbonate linkers, or protected phenol intermediates that later undergo deprotection under controlled conditions, enabling attachment to biomolecular targets. The D-amino acid backbone and alpha-methyl substitution provide a means to control stereochemical presentation of the aromatic side chain during conjugate synthesis. Downstream derivatives can be used to generate labeled peptide probes, affinity tags, or biomolecule-modifying reagents for studying molecular recognition and binding kinetics in vitro.

4. Protected Amino Acid Chemistry

H-alpha-Me-D-Tyr-OH functions as a chiral starting material for preparing N-protected amino acid derivatives and side-chain-protected tyrosine building blocks used in peptide manufacturing and synthesis planning. The free carboxylic acid supports formation of activated C-terminal forms after conversion to protected amino acid intermediates, while the phenolic group can be temporarily masked to prevent undesired reactions during peptide coupling. The alpha-methyl stereocenter provides stereochemical fidelity through protection/deprotection sequences, supporting consistent incorporation of the D residue into longer constructs. Prepared protected forms derived from H-alpha-Me-D-Tyr-OH can serve as process-ready inputs for fine chemical synthesis, enabling reproducible peptide coupling chemistry across multiple batch runs.

5. Analytical Research Standards

H-alpha-Me-D-Tyr-OH is suitable for analytical research where stereodefined amino acid standards or calibration components are required to monitor derivatization, coupling outcomes, or stereochemical integrity. The combination of D-configuration, alpha-methyl substitution, and phenolic side chain provides a distinct chromatographic and mass spectrometric signature relative to natural L-tyrosine derivatives. The phenol can be used to generate predictable derivatives for detection methods, while the carboxylic acid supports derivatization schemes compatible with LC-MS or GC-MS workflows. Stereochemically defined reference materials prepared from H-alpha-Me-D-Tyr-OH can support method development for peptide hydrolysis analysis, amino acid profiling, and quality control of unnatural amino acid-containing products.

6. Industrial Fine Chemical Synthesis

H-alpha-Me-D-Tyr-OH can be applied in industrial fine chemical synthesis as a chiral amino acid intermediate feeding into protected amino acid production and downstream specialty peptide or peptidomimetic manufacturing. The presence of a free carboxylic acid and a phenolic side chain enables conversion into protected, coupling-ready derivatives that align with scalable peptide intermediate supply chains. Alpha-methylation and D stereochemistry can be used to prepare stereochemically consistent building blocks for manufacturing routes that require controlled backbone substitution patterns. The resulting intermediates support batch-to-batch reproducibility in industrial synthesis of non-natural amino acid-containing peptides and related functional molecules.

1. Spatiotemporal delivery of nanoformulated liraglutide for cardiac regeneration after myocardial infarction

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

3. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

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

5. Tachykinin-related peptides modulate immune-gene expression in the mealworm beetle Tenebrio molitor L