Erythro-DL-β-Hydroxynorleucine is a non-proteinogenic, β-hydroxylated amino acid derivative of norleucine featuring an aliphatic side chain bearing a hydroxyl group at the β-position and a stereochemical relationship consistent with the erythro diastereomeric form. The molecule contains a free amino group and a carboxyl group characteristic of amino acids, and the β-hydroxyl functionality provides an additional hydrogen-bonding and polarity element that can participate in conformational effects and chemical derivatization, with the "DL" designation indicating a racemic mixture of stereoisomers at the relevant stereocenters. In peptide chemistry and chemical biology, it is used as a building block to introduce β-hydroxy motifs into peptide analogues for structure-activity studies, protein engineering experiments, and analytical labeling or conjugation workflows where a hydroxyl handle is required.
CAT No: CP07202
Erythro-DL-β-Hydroxynorleucine is a β-hydroxy amino acid derivative featuring a straight-chain norleucine backbone bearing a stereodefined β-hydroxyl group in the erythro relationship to the α-amino stereocenter. The compound contains a primary amino functionality and a carboxylic acid (or acid form depending on supplied grade), enabling standard amino acid coupling chemistry and downstream conversion to protected amino acid intermediates. The β-hydroxyl group provides an additional handle for esterification, ether formation, oxidation to carbonyl derivatives, and selective protection strategies that can be orthogonal to the amino and carboxyl groups. The presence of DL stereochemistry indicates racemic material with both erythro enantiomers, which is useful for process screening, method development, and generating diastereomeric outcomes in peptide or peptidomimetic synthesis.
1. Peptide Synthesis
Erythro-DL-β-Hydroxynorleucine is applied in peptide building-block preparation where the α-amino and carboxyl functionalities support amide bond formation under peptide coupling conditions. The β-hydroxyl side chain can be protected as an ether or ester to control chemoselectivity during N-protection, C-terminal activation, and sequential chain elongation. Erythro stereochemical placement of the hydroxyl relative to the backbone can influence local conformational preferences in peptide analogs and can be leveraged to probe stereochemical effects on folding or recognition. Racemic availability can facilitate rapid synthesis of hydroxylated peptide libraries and can also serve as an intermediate for later stereochemical resolution or chiral derivatization workflows.
2. Side-Chain Functionalization
Erythro-DL-β-Hydroxynorleucine is used as a functionalized amino acid intermediate for side-chain derivatization in synthetic organic chemistry and chemical biology. The β-hydroxyl group can undergo protection/deprotection cycles, selective oxidation to β-keto or related carbonyl motifs, and conversion to leaving-group activated intermediates for substitution chemistry. The amino acid framework enables formation of amide or ester derivatives that retain a handle for further elaboration while maintaining compatibility with downstream coupling steps. Downstream products can include hydroxyl-bearing peptidomimetics, β-functionalized analogs for receptor or enzyme binding studies, and platform intermediates for assembling larger heteroatom-rich scaffolds.
3. Chiral Amino Acid Intermediate
Erythro-DL-β-Hydroxynorleucine is suitable as a chiral amino acid precursor in workflows that require access to β-hydroxy stereochemistry for method development and stereochemical control. The erythro relationship provides a defined relative stereochemical motif that can be carried through to protected amino acid derivatives and then into peptide coupling or derivatization sequences. Racemic DL material can be employed to evaluate resolution strategies, diastereomeric formation during coupling, or selective transformations that differentiate enantiomers at later stages. The compound's amino acid functionality supports conversion to N-protected and C-activated forms, enabling its use as a standardized intermediate in stereoselective synthesis campaigns and fine chemical production planning.
4. Peptidomimetics And SAR Studies
Erythro-DL-β-Hydroxynorleucine is utilized in peptidomimetic construction where hydroxylated side chains help emulate hydrogen-bonding patterns and polar surface features typical of bioactive peptide regions. The β-hydroxyl can be used to tune polarity, introduce conformational constraints via protected ether/ester variants, or serve as a precursor to carbonyl-containing analogs for structure-activity relationship studies. The amino acid backbone supports incorporation into constrained analogs through amide linkages, while N- and O-protection strategies enable sequential assembly of multi-functional scaffolds. Racemic input can support SAR mapping by generating stereochemically mixed analog sets for screening and subsequent refinement through stereopure synthesis.
5. Analytical Research Standards
Erythro-DL-β-Hydroxynorleucine is applicable as an analytical reference material and biochemical research intermediate for method validation in amino acid and peptide analytics. The β-hydroxyl functionality and amino acid backbone provide characteristic chromatographic and mass spectrometric signatures, supporting quantitation of hydroxylated amino acid derivatives and monitoring of derivatization steps. Protected derivatives derived from the amino and hydroxyl groups can be used to develop targeted LC-MS/MS transitions for peptide building-block verification and for tracking side-chain protection efficiency. The compound's stereochemical motif supports studies that distinguish β-hydroxy stereochemistry in synthetic monitoring, impurity profiling, and stability assessment of hydroxylated intermediates during process development.
6. Pharmaceutical Intermediate Preparation
Erythro-DL-β-Hydroxynorleucine is relevant to pharmaceutical intermediate preparation where hydroxylated amino acid building blocks are required for constructing polar, stereochemically defined motifs in peptide-like or peptidomimetic candidates. The α-amino and carboxylic acid functionalities enable conversion to N-protected amino acid derivatives and activated C-terminal forms suitable for controlled amide coupling in manufacturing-oriented synthetic routes. The β-hydroxyl group can be managed through orthogonal protection strategies to allow sequential transformations and minimize undesired side reactions during scale-up. Downstream formation of hydroxyl-stabilized analogs, protected intermediates for fragment assembly, and impurity-controlled synthetic sequences aligns with industrial chemical manufacturing needs for robust amino acid derivative workflows.
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