N-Boc-S-2-Pyridinylthio-L-cysteine is a cysteine derivative bearing a pyridinylthio substituent that modulates redox behavior and thiol reactivity. The residue is used to install reversible disulfide-like linkages and explore metal coordination. Researchers apply it in redox-sensitive peptide engineering. Its protective Boc group aids controlled synthesis.
CAT No: R2133
CAS No:117310-07-3
Synonyms/Alias:N-Boc-S-2-Pyridinylthio-L-cysteine;(2R)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-(pyridin-2-yldisulfanyl)propanoic acid;117310-07-3;
N-Boc-S-2-Pyridinylthio-L-cysteine is a synthetic amino acid derivative featuring a tert-butyloxycarbonyl (Boc) protecting group on the amino terminus and a 2-pyridinylthio moiety on the sulfur atom of the cysteine side chain. As a structurally modified cysteine, it serves as a valuable building block in peptide chemistry and organic synthesis, offering both selective reactivity and functional versatility. Its unique combination of protection and functionalization enables precise manipulation during multi-step synthetic protocols, making it highly relevant for research in peptide modification, bioconjugation strategies, and the development of novel biomolecules.
Peptide Synthesis: In solid-phase peptide synthesis (SPPS) and solution-phase methodologies, N-Boc-S-2-Pyridinylthio-L-cysteine is frequently utilized as a protected cysteine residue. The Boc group safeguards the α-amino function, while the 2-pyridinylthio modification confers orthogonal protection to the thiol side chain. This dual-protection strategy allows for the sequential assembly of complex peptides and facilitates site-specific introduction of cysteine residues with enhanced control over side-chain reactivity. Researchers exploit these properties to minimize undesired side reactions and to enable selective deprotection steps at later stages of synthesis.
Disulfide Bridge Engineering: The 2-pyridinylthio functionality on the cysteine sulfur atom is particularly advantageous for controlled disulfide bond formation in synthetic peptides and proteins. Upon mild activation, the pyridinylthio group can be displaced to generate a reactive thiol, which can then participate in chemoselective disulfide coupling. This approach is instrumental in the assembly of proteins with native or engineered disulfide architectures, supporting studies on protein folding, stability, and structure-function relationships.
Bioconjugation and Site-Specific Labeling: The unique reactivity of the S-2-pyridinylthio group enables site-specific conjugation of peptides or proteins to a wide range of functional probes, polymers, or affinity tags. Through nucleophilic displacement or thiol exchange reactions, this derivative allows for the attachment of fluorescent labels, biotin, or other functional moieties at predetermined positions. Such site-directed labeling is essential for the development of advanced biomolecular tools used in imaging, affinity purification, and biosensor applications.
Chemical Ligation Strategies: N-Boc-S-2-Pyridinylthio-L-cysteine is a valuable component in native chemical ligation (NCL) and related chemoselective coupling techniques. Its protected thiol can be unmasked under controlled conditions to participate in ligation reactions with thioesters or other activated species, enabling the assembly of large peptides and proteins from unprotected fragments. The precise control over thiol reactivity provided by the pyridinylthio group enhances the efficiency and selectivity of these ligation processes, thereby expanding the scope of synthetic protein chemistry.
Analytical and Mechanistic Studies: The incorporation of this modified cysteine into peptides or small molecules provides a versatile handle for mechanistic investigations of thiol-based reactivity, redox processes, and sulfur transfer reactions. The distinct electronic and steric properties of the 2-pyridinylthio substituent facilitate studies on thiol activation, nucleophilicity, and the influence of side-chain modifications on peptide behavior. Such research contributes to a deeper understanding of cysteine chemistry and informs the design of novel bioactive peptides and functionalized biomaterials.
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