DL-6-Hydroxynorleucine is a non-proteinogenic, aliphatic amino acid derivative featuring a six-carbon side chain bearing a terminal hydroxyl substituent (6-hydroxy) and a free amino group and carboxyl group characteristic of amino acids. The molecule is supplied as a DL mixture, providing both stereochemical configurations at the chiral center associated with the amino acid backbone, and the side-chain hydroxyl enables hydrogen-bonding and can participate in derivatization or polarity modulation during peptide synthesis. In research workflows, it is employed as a building block for preparing peptides and structure-activity analogues that probe the effects of introducing a hydroxyl-bearing aliphatic residue, as well as for chemical labeling and analytical method development where an alcohol functional handle is required.
CAT No: CP07301
DL-6-Hydroxynorleucine is a hydroxylated, unbranched amino acid derivative corresponding to a norleucine backbone bearing a secondary alcohol at the 6-position relative to the amino acid stereocenter. The molecule contains an amino group and a carboxylic acid (or, depending on the supplied form, a corresponding protected/activated functionality), with the side-chain hydroxyl providing a hydrogen-bonding handle and enabling selective derivatization. The DL designation indicates a racemic mixture at the stereogenic center, which is relevant for studies requiring matched enantiomeric controls or for downstream resolution to obtain single-enantiomer building blocks. The presence of a free or protected alcohol and the amino acid functionality makes the compound suitable for peptide coupling chemistry and for conversion into protected amino acid intermediates used in synthetic organic and biochemical research.
1. Peptide Synthesis
DL-6-Hydroxynorleucine is applied in peptide assembly workflows where a side-chain hydroxyl is incorporated as a functional motif for hydrogen-bonding and post-coupling modification. The amino acid backbone supports standard amide bond formation, while the side-chain alcohol can be protected (for example, as an ether or silyl-type group) to maintain compatibility with coupling reagents and base-stable peptide synthesis conditions. Racemic DL material can be used for generating hydroxyl-containing peptide analog libraries, with later stereochemical separation when enantiopurity is required for structure-activity relationship studies. Downstream, hydroxyl-bearing peptide products can be used as substrates for enzymatic assays or as intermediates for further functional group transformations.
2. Amino Acid Derivatization
DL-6-Hydroxynorleucine is suitable for amino acid derivatization strategies that exploit the side-chain secondary alcohol for controlled functionalization. The hydroxyl group can be converted into esters, carbamates, or ether derivatives, enabling tuning of polarity, protecting-group stability, and reactivity toward subsequent synthetic steps. The carboxylic acid and amino functionality support formation of activated derivatives used in chiral building block development, including conversion to protected amino acid intermediates for sequential synthesis. Racemic input can be leveraged for rapid generation of derivative sets, while stereochemical resolution may be applied when single-enantiomer alcohol reactivity or stereoelectronic effects are targeted.
3. Bioconjugation Chemistry
DL-6-Hydroxynorleucine is used in chemical biology and biomolecule modification contexts where an amino acid side-chain hydroxyl can serve as a handle for conjugation-compatible linkers and post-functionalization. The amino acid framework can be incorporated into peptides or peptide-like scaffolds that present the hydroxyl group at a defined spatial position for subsequent coupling to electrophiles or for attachment of solubilizing or affinity tags. Protecting-group strategies that mask the amino and carboxyl groups during scaffold assembly can be paired with selective deprotection to expose the hydroxyl for controlled conjugation chemistry. DL stereochemistry can be employed for comparative labeling studies, with enantiomer-specific variants prepared when stereochemical recognition by biomolecular targets is a key variable.
4. Enzyme Substrate Studies
DL-6-Hydroxynorleucine is applied to enzyme substrate and inhibitor design research where a hydroxylated side chain can influence binding through hydrogen bonding and conformational effects. The amino acid's ability to be incorporated into peptide substrates enables evaluation of enzyme tolerance toward secondary alcohol functionalities and can support mechanistic studies using analogs with protected or derivatized hydroxyl groups. Racemic DL material can be used to probe whether the enzyme exhibits stereochemical preference, with downstream resolution to isolate the active enantiomer for follow-on studies. The resulting hydroxyl-bearing peptide or amino acid derivatives can function as analytical standards and as biochemical research intermediates for mapping substrate specificity.
5. Pharmaceutical Intermediate Preparation
DL-6-Hydroxynorleucine is relevant to pharmaceutical intermediate preparation and fine chemical synthesis routes that require hydroxyl-functional amino acid building blocks for medicinal chemistry programs. The compound's amino acid functionality can be transformed into N-protected and/or C-activated forms to enable incorporation into peptide-like fragments, peptidomimetic scaffolds, or hydroxyl-containing side chains in structure-activity relationship studies. The side-chain hydroxyl supports downstream conversion into functional groups commonly used in medicinal chemistry, including protected alcohol intermediates that survive coupling steps and can be selectively unmasked later. Racemic supply can support parallel synthesis and process development screening, while stereoselective steps can be introduced when a single-enantiomer intermediate is required for final scaffold construction.
6. Process Chemistry Intermediate
DL-6-Hydroxynorleucine is suitable for process chemistry intermediate development because it contains orthogonal functional elements that can be protected, activated, and carried through multistep manufacturing sequences. The amino and carboxyl groups enable formation of coupling-ready derivatives, while the side-chain hydroxyl can be managed through robust protecting-group selection to ensure controlled reactivity during peptide coupling or fragment assembly. DL stereochemistry can reduce upstream complexity for route scouting and scale-up of hydroxyl-bearing intermediates, with later stereochemical adjustment performed via resolution or stereoselective conversion if needed. The hydroxyl-functional amino acid thus serves as a practical feedstock for producing protected amino acid derivatives and peptide building block precursors used in specialty chemical production and industrial chemical manufacturing.
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