DL-Lanthionine is a sulfur-containing, non-proteinogenic amino acid derivative classified as a thioether-linked amino acid in which two carbon skeletons are connected through a thioether (-S-) bridge rather than a disulfide. The molecule contains both an amino group and a carboxyl group, and the DL designation indicates a racemic mixture of stereoisomers at the amino acid stereocenters when present. DL-Lanthionine is used as a defined building block for peptide and thioether bond studies, including the preparation of lanthionine-containing peptide analogues and related structure-activity or chemical labeling experiments where a stable thioether linkage is required.
CAT No: CP07801
DL-Lanthionine is a thioether-containing amino acid derivative with a characteristic lanthionine skeleton formed by two sulfur atoms linking amino acid side chains, yielding a rigid, thioether-bridged framework. The molecule bears an amino group and a carboxylic acid (or acid/base salt forms depending on handling), and its thioether linkage confers reduced oxidation sensitivity relative to thiols while providing distinct sulfur-based reactivity for downstream derivatization. DL-Lanthionine is supplied as a racemic mixture (DL), enabling stereochemically defined studies when paired with chiral resolution or stereospecific transformations. The combination of sulfur-rich functionality and amino acid handles makes DL-Lanthionine a practical intermediate for peptide chemistry, sulfur incorporation strategies, and sulfur-bridged scaffold construction.
1. Peptide Synthesis
DL-Lanthionine is applied in peptide synthesis workflows that require incorporation of sulfur-bridged motifs or lanthionine-like crosslinks into peptide backbones. The amino and carboxyl functionalities support coupling chemistry, while the thioether bridge can be retained as a stable linkage during peptide assembly, enabling construction of thioether-constrained peptide analogs. Protection-group strategies typically focus on managing the amino and carboxyl groups during coupling, with the sulfur bridge functioning as a structural element rather than a transient protecting group. Downstream, DL-Lanthionine-derived fragments can be used to generate peptide building blocks for studying crosslink effects on conformation, stability, and fragmentation behavior in synthetic peptide science.
2. Peptidomimetics
DL-Lanthionine is utilized in peptidomimetic and molecular scaffold design programs that seek rigidification through thioether-bridged geometry. The lanthionine thioether linkage provides a sulfur-rich, conformationally restricting element that can be embedded into analogs to modulate backbone flexibility and intramolecular packing. Amino acid functional groups enable further derivatization into protected intermediates suitable for sequential coupling, allowing systematic exploration of how sulfur-bridged constraints affect physicochemical properties and binding-site complementarity. Synthetic routes can leverage DL-Lanthionine as a chiral or racemic sulfur-containing unit, supporting structure-activity relationship studies across libraries of lanthionine-inspired peptidomimetics.
3. Chemical Biology Probes
DL-Lanthionine is suitable for chemical biology research where sulfur-containing amino acid derivatives are needed for probe construction, affinity handles, or controlled conjugation chemistry. The thioether linkage can be used as a stable sulfur motif within labeled peptides or biomolecule-reactive constructs, while the amino acid termini facilitate conversion into activated intermediates for attachment to targeting scaffolds. Derivatization can be directed toward introducing reporter groups, linkers, or capture moieties without disrupting the thioether bridge, supporting reproducible labeling strategies in biochemical workflows. Racemic DL material may be employed for general probe development, while stereodefined analogs can be prepared through resolution or stereoselective downstream transformations when stereochemical effects on recognition are investigated.
4. Analytical Standards
DL-Lanthionine is employed as an analytical reference material for method development and characterization of sulfur-containing amino acid derivatives in chromatography and mass spectrometry. The defined lanthionine thioether structure produces characteristic fragmentation patterns and retention behavior, enabling identification of related crosslinked species in synthetic mixtures or biological matrices. Amino and carboxyl functionalities allow preparation of salts or derivatized forms that improve detectability under specific analytical conditions. Downstream, DL-Lanthionine standards support quality control of peptide synthesis intermediates, verification of lanthionine incorporation, and calibration of quantitation workflows for sulfur-bridged analytes.
5. Process Chemistry Intermediate
DL-Lanthionine serves as a practical intermediate in process chemistry for manufacturing sulfur-bridged building blocks and fine chemical intermediates. The stable thioether bridge reduces susceptibility to oxidation compared with thiol-containing analogs, supporting robust handling across multi-step synthesis where amino acid protection and activation cycles are used. Amino acid functional groups enable conversion into protected derivatives or activated coupling forms that integrate into larger synthetic sequences, including peptide fragment assembly and scaffold elaboration. Industrial relevance is supported by the molecule's role as a defined sulfur-containing unit for producing lanthionine-inspired intermediates used in peptide science, specialty chemical production, and applied synthetic methodology development.
6. Side-Chain Functionalization
DL-Lanthionine is suitable for side-chain functionalization strategies that transform its sulfur-rich framework into tailored thioether-bearing derivatives. The thioether linkage provides a platform for selective chemical modifications that can introduce electrophiles, linkers, or additional functional groups while maintaining the core lanthionine scaffold for subsequent coupling. Amino and carboxyl groups can be protected or activated to control chemoselectivity during derivatization, enabling stepwise synthesis toward N- or C-terminally modified analogs. Downstream utility includes generating functionalized amino acid intermediates for peptide coupling chemistry, biomolecule conjugation reagents, and sulfur-bridged materials where controlled sulfur incorporation is required in applied chemical manufacturing.
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