Erythro-L-β-Hydroxynorleucine is a non-proteinogenic, β-hydroxy-substituted amino acid featuring a straight-chain norleucine backbone with a secondary hydroxyl group at the β-position and an amino acid side chain that can participate in hydrogen bonding and polarity modulation. The molecule contains a primary amino group and a carboxyl group, and its "erythro" designation specifies the relative stereochemistry between the β-hydroxyl substituent and the amino-acid framework, while the "L" prefix indicates the absolute configuration at the α-carbon. As a β-hydroxy amino acid analogue, it is used in peptide chemistry and structure-activity studies to probe how β-hydroxyl functionality and stereochemical geometry influence peptide conformation, hydrogen-bonding patterns, and chemical reactivity during synthesis of modified peptide analogues.
CAT No: CP07205
Erythro-L-β-Hydroxynorleucine is an L-configuration amino acid derivative featuring a β-hydroxylated side chain on a norleucine backbone, with erythro stereochemistry across the β-hydroxy and the α-amino-bearing framework. The molecule presents a primary amino functionality and a carboxylic acid (or, depending on the supplied form, a corresponding protected/activated derivative), enabling standard amino acid coupling chemistry while also providing a stereodefined secondary alcohol for selective functional transformations. The β-hydroxyl group can participate in hydrogen-bonding and can be protected as ethers or esters to control chemoselectivity during peptide assembly and downstream derivatization. As a chiral amino acid building block and biochemical research intermediate, erythro-L-β-hydroxynorleucine can be incorporated into peptide sequences or converted into protected forms that support iterative synthesis and stereochemically consistent side-chain modification.
1. Peptide Synthesis
Erythro-L-β-Hydroxynorleucine is used in peptide synthesis workflows where a stereodefined β-hydroxy side chain is required for conformational bias and hydrogen-bonding interactions. The L-amino acid framework supports N- and C-terminal protection strategies, while the erythro-configured β-alcohol can be masked (for example as an ether or ester) to withstand peptide coupling conditions and then unmasked under controlled deprotection. The resulting protected amino acid derivative can be activated for amide bond formation using standard peptide coupling chemistries, enabling incorporation as a residue that preserves side-chain stereochemistry. Downstream, the hydroxyl functionality can be carried into peptide analog libraries, fragment coupling studies, and structure-guided optimization of peptide-like scaffolds.
2. Peptidomimetics And SAR
Erythro-L-β-Hydroxynorleucine is applied in peptidomimetic construction and structure-activity relationship studies where a β-hydroxy stereocenter functions as a polar motif for receptor or enzyme recognition. The secondary alcohol and the extended norleucine-like side chain can be derivatized into protected intermediates that maintain stereochemical integrity during scaffold assembly, supporting SAR-driven replacement of natural residues. Side-chain functional group interconversion, including conversion to leaving groups, carbonate/ester derivatives, or protected alcohol analogs, can be used to generate focused sets of analogs for binding and mechanistic comparisons. The amino acid's chiral center and hydrogen-bonding capacity make it suitable for fragment-based molecular design and for preparing stereochemically defined analogs that probe the role of β-hydroxyl geometry.
3. Chemical Biology Labeling
Erythro-L-β-Hydroxynorleucine is suitable for chemical biology research aimed at building stereochemically defined probes and conjugatable peptide fragments. The β-hydroxyl group can be selectively protected during synthesis and later functionalized into handle-bearing derivatives (such as activated esters or ether-linked groups) for attachment to carriers, affinity tags, or biomolecule scaffolds. The amino acid backbone supports incorporation into peptides or peptide-like constructs, enabling site-specific presentation of the functionalized side chain with controlled stereochemistry. Downstream applications include preparation of labeled biomolecular intermediates for interaction mapping, pathway studies, and analytical assay development that depend on consistent chiral presentation of a hydroxylated residue.
4. Protein Engineering Intermediates
Erythro-L-β-Hydroxynorleucine is utilized as a chiral amino acid intermediate for protein engineering and synthetic protein studies where hydroxylated side-chain chemistry is required. The L-configuration and erythro stereochemistry enable consistent placement of a β-hydroxy motif that can influence local structure, solvent interactions, and post-synthetic chemical modification. N-protection and side-chain protection strategies allow the residue to be incorporated into peptide segments used for semisynthesis, ligation-compatible fragments, or recombinant protein modification workflows that rely on defined chemical handles. The hydroxyl-bearing side chain can subsequently be transformed into stable derivatives that support downstream conjugation, crosslinking chemistry, or controlled functional group installation on engineered protein constructs.
5. Process Chemistry Intermediate
Erythro-L-β-Hydroxynorleucine is relevant to process chemistry and fine chemical synthesis as a stereochemically defined chiral intermediate for manufacturing peptide building blocks and hydroxyl-functional amino acid derivatives. The presence of an alcohol and amino acid functional set supports route design that uses orthogonal protection schemes to manage chemoselectivity during activation, coupling, and purification steps. The erythro stereochemistry provides a defined stereochemical outcome that can reduce variability in downstream peptide analog synthesis when the β-hydroxy motif is retained. The compound can be converted into protected amino acid forms suitable for industrial peptide manufacturing, enabling consistent feedstock preparation for specialty chemical production and applied amino acid derivatization programs.
6. Analytical Standards Development
Erythro-L-β-Hydroxynorleucine is applied in analytical research as a chiral reference material and derivatization precursor for monitoring amino acid incorporation and side-chain modification. The β-hydroxyl functionality enables derivatization strategies that improve chromatographic behavior or detection sensitivity while preserving stereochemical information, supporting method development for amino acid analysis in peptide-derived samples. The L-amino acid structure also supports preparation of labeled or protected derivatives that can serve as internal standards or calibration components for quantifying hydroxylated residues. Downstream, the compound's defined stereochemistry supports reliable interpretation of stereochemical outcomes in peptide synthesis, degradation studies, and quality control of hydroxyl-bearing peptide intermediates.
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