H-D-Lys(N3)-OH*HCl

H-D-Lys(N3)-OH*HCl is the hydrochloride salt of an L-lysine derivative bearing a side-chain azide (N3) and a free carboxylic acid, with the alpha-amino functionality protected as the Nα-deuterated amino acid (H at the alpha carbon is replaced by deuterium). The molecule retains the lysine backbone stereochemistry at the chiral center, providing a well-defined spatial arrangement for peptide coupling chemistry while introducing a chemically orthogonal azide handle on the ε-amino side chain. The azide group is stable under many peptide-manipulation conditions yet can participate in strain-promoted or copper-mediated azide-alkyne cycloaddition, enabling downstream conjugation and labeling workflows. The carboxylic acid and deuterated amino acid framework make the compound suitable as a protected or derivatizable amino acid intermediate for synthesis of azide-functionalized peptides and for mechanistic studies where isotopic substitution at the alpha position is informative.

1. Peptide Synthesis

H-D-Lys(N3)-OH*HCl is applied in peptide building workflows where lysine-residue incorporation is required alongside a latent azide functionality for later diversification. The side-chain azide on the ε-position enables post-coupling functionalization without disturbing the peptide backbone, while the free carboxylic acid and amino group support standard amino acid activation and coupling strategies used in protected amino acid chemistry. The Nα-deuteration can be leveraged to track incorporation, monitor fragment-level transformations by mass spectrometry, or support stereochemical and mechanistic studies during peptide assembly. The resulting azide-bearing lysine residue can be carried through peptide coupling, deprotection, and subsequent click-compatible derivatization to generate azide-functional peptide analogs for research-grade scaffold construction.

2. Bioconjugation Chemistry

H-D-Lys(N3)-OH*HCl serves as a chiral azide-bearing amino acid intermediate for bioconjugation and chemical biology labeling schemes that rely on orthogonal reactive handles. The ε-azide provides a defined conjugation site for attaching probes, affinity tags, or biomolecule-reactive moieties through azide-alkyne cycloaddition, while the lysine backbone supports incorporation into peptide conjugates or linker architectures. The hydrochloride salt form facilitates handling and can support controlled salt-state behavior during synthetic steps that require amino acid solubility management. Downstream, azide-functional lysine constructs derived from this intermediate can be used to generate conjugation-ready peptide reagents and to prepare labeled biomolecular tools for mechanistic and analytical studies.

3. Isotope-Labeling Studies

H-D-Lys(N3)-OH*HCl is suitable for isotope-labeling applications where deuterium at the alpha position provides a stable tracer for mass-based detection and kinetic or mechanistic interpretation. The deuterated amino acid framework can be incorporated into peptides or peptidomimetics, allowing researchers to follow incorporation sites, monitor fragmentation patterns, or distinguish labeled species during LC-MS/MS analysis. The side-chain azide enables orthogonal post-synthetic modification, so labeled constructs can be diversified while maintaining the isotopic label for downstream detection. The combination of azide chemistry and alpha-deuteration supports analytical research intermediate preparation for studies that require both a reactive handle and a spectroscopically informative label.

4. Side-Chain Functionalization

H-D-Lys(N3)-OH*HCl is used in amino acid modification programs that target lysine side-chain derivatization while preserving a functional group for subsequent transformations. The ε-azide can be converted into a wide range of triazole-linked motifs via click chemistry, enabling generation of functional analogs such as linker-bearing peptides, affinity reagents, or chemically tagged building blocks. The free carboxylic acid and stereodefined lysine backbone support conversion into activated derivatives for incorporation into larger synthetic sequences, including peptide analog construction and fragment assembly. Downstream derivatization of the azide handle allows controlled introduction of polarity, sterics, and binding-site features that are relevant to structure-function investigations in peptide science and chemical biology.

5. Pharmaceutical Intermediate Preparation

H-D-Lys(N3)-OH*HCl is applicable to pharmaceutical intermediate workflows where azide-functional amino acid derivatives are needed for constructing drug-like peptidomimetics, linker systems, or scaffold-building blocks. The lysine-derived stereocenter and functional groups enable stepwise synthesis of protected amino acid derivatives and subsequent peptide coupling or amide formation in a manner compatible with industrial fine chemical synthesis planning. The azide group functions as a protected reactive handle that can be carried through multiple transformations and then converted late in the synthetic route to install conjugatable or pharmacophore-adjacent fragments. The deuterated alpha position can further support route development and analytical qualification strategies where labeled intermediates or reference standards are beneficial for process monitoring and structural confirmation.

1. Immune-awakening Saccharomyces-inspired nanocarrier for oral target delivery to lymph and tumors

2. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment

3. Proinsulin C-peptide and insulin: Limited pattern similarities of interest in inter-peptide interactions but no C-peptide effect on insulin and IGF-1 receptor signaling

4. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function

5. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes