L-Allo-δ-Hydroxylysine HCl is a free, proteinogenic amino acid derivative in which the side chain bears a δ-hydroxyl substituent on the lysine framework, with the amino acid present as the hydrochloride salt. The molecule contains both an amino group and a carboxyl group on the α-carbon, while the side-chain hydroxyl provides an additional hydrogen-bonding and polar functionality that can participate in chemical derivatization or coordination chemistry. As an amino acid building block, it is used for peptide and amino acid derivative synthesis and for chemical biology or analytical workflows that require a hydroxylysine-containing residue with a defined side-chain hydroxyl functionality.
CAT No: CP07103
L-Allo-δ-Hydroxylysine HCl contains the lysine backbone with an additional δ-hydroxyl functional group, providing a stereodefined chiral amino acid framework suitable for amino acid derivatization and peptide chemistry. The side-chain hydroxyl enables hydrogen-bonding and can be selectively protected or converted to reactive leaving groups for downstream coupling or conjugation. The hydrochloride salt form improves handling and can influence salt-dependent solubility during protected amino acid synthesis and analytical workflows. The allo configuration at the δ-position relative to the lysine side chain stereochemistry supports stereochemically controlled incorporation into peptide analogs and biochemical research intermediates where hydroxylated lysine motifs are required.
1. Peptide Synthesis
L-Allo-δ-Hydroxylysine HCl is applied in peptide building block preparation where the α-amino and α-carboxyl functionalities participate in standard peptide coupling chemistry after appropriate protection and activation. The δ-hydroxyl side chain can be protected as an ether or acyl group to prevent side reactions during amide bond formation, then deprotected to regenerate the free hydroxylysine functionality for subsequent steps. The allo stereochemistry supports incorporation of hydroxylated lysine motifs into peptides used to probe recognition events that depend on side-chain stereochemistry and hydrogen-bonding patterns. L-Allo-δ-Hydroxylysine HCl can therefore serve as a chemically defined intermediate for constructing hydroxylated peptide sequences and peptidomimetic scaffolds.
2. Chemical Biology
L-Allo-δ-Hydroxylysine HCl is utilized in chemical biology research to generate hydroxylated lysine-containing probes, affinity tags, and enzyme-substrate analogs that report on recognition of modified lysine residues. The side-chain hydroxyl enables controlled derivatization to linkers, fluorescent handles, or capture moieties while maintaining the stereochemical context of the allo-hydroxylysine motif. Salt-state handling as the hydrochloride can support reproducible reagent preparation for conjugation chemistry and for building defined molecular tools. L-Allo-δ-Hydroxylysine HCl can be employed as an amino acid-based intermediate for studying post-translational modification chemistry, molecular recognition, and structure-dependent binding in biomolecular assays.
3. Side-Chain Functionalization
L-Allo-δ-Hydroxylysine HCl is suitable for side-chain functionalization workflows that convert the δ-hydroxyl into protected intermediates or reactive derivatives for subsequent synthetic transformations. The hydroxyl group can be selectively protected to enable orthogonal deprotection strategies relative to α-amino and α-carboxyl groups, supporting stepwise synthesis of complex amino acid derivatives and peptide conjugates. The presence of the lysine primary amine allows sequential derivatization planning, including N-protection for chemoselective reactions and later functional group unveiling for coupling or labeling. L-Allo-δ-Hydroxylysine HCl thereby functions as a stereodefined chiral amino acid intermediate for producing hydroxylated lysine derivatives used in synthetic organic chemistry and biochemical reagent development.
4. Protein Engineering
L-Allo-δ-Hydroxylysine HCl can be applied in protein engineering programs that require defined incorporation of hydroxylated lysine analogs into peptides used to model or interrogate protein surfaces. The α-amino acid functionality supports attachment into peptide segments that mimic hydroxylated lysine microenvironments, while the δ-hydroxyl provides hydrogen-bonding capability that can influence local conformation and intermolecular interactions. The allo stereochemistry helps maintain a specific spatial arrangement of the hydroxyl relative to the lysine side chain, which can be critical when comparing structure-function relationships across stereoisomeric analogs. L-Allo-δ-Hydroxylysine HCl can serve as a defined intermediate for generating protein-mimetic constructs, binding studies, and mechanistic probes in applied protein chemistry.
5. Pharmaceutical Intermediate Preparation
L-Allo-δ-Hydroxylysine HCl is relevant to pharmaceutical intermediate preparation for manufacturing routes that require hydroxylated amino acid motifs as building blocks in peptidomimetic and constrained ligand synthesis. The protected amino acid derivative strategy can leverage orthogonal protection of the δ-hydroxyl to enable selective functional group transformations without disturbing the core amino acid functionality during sequence assembly or fragment coupling. The hydrochloride salt form can support consistent handling in fine chemical synthesis where reproducible solubility and salt formation are practical considerations for scale-up. L-Allo-δ-Hydroxylysine HCl can therefore be employed as a chiral, stereochemically defined intermediate for producing hydroxylated lysine-containing scaffolds used downstream in medicinal chemistry and specialized manufacturing of peptide-based molecules.
6. Analytical Research Standards
L-Allo-δ-Hydroxylysine HCl is used in analytical research as a chemically defined reference material for method development and calibration in workflows targeting hydroxylated lysine residues. The distinct δ-hydroxyl functionality and allo stereochemistry provide a characteristic chemical signature for chromatographic separation and derivatization-based detection strategies. The amino acid salt form can facilitate reproducible preparation of standards for mass spectrometry, amino acid profiling, and peptide hydrolysate analysis where stereochemical specificity matters. L-Allo-δ-Hydroxylysine HCl can be applied to support accurate quantitation and structural confirmation of hydroxylated lysine-containing analytes in biochemical and industrial monitoring contexts.
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