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Disulfide Bonds 

Disulfide Bridge Peptides
Synpeptide Co Ltd have synthesized over 8000 disulfide-containing peptides successfully  so far.
1, Synthesis of your peptide having:
    intrachain and/or interchain disulfide bond(s),
    single to five or more disulfide bond(s),
    a long peptide backbone with intrachain disulfide bond(s), and disulfide bond(s) in combination with stable isot    -ope or fluorescencelabeling and/or other various modifications.
2, Regioselective formation of two or three disulfide linkages.
3, Formation of homo-and/or hetero-disulfide bond(s) between non-cysteine sulfur-containing amino acid derivatives including deamino compounds.
   Selective disulfide bond formation

Cysteine (Cys) residues in proteins and peptides are capable of forming disulfide bonds (i.e., disulfide bridges), a reversible covalent linkage between two side chain thiol groups. Disulfide bonds confer conformational constraints in linear peptide sequences that molecular rigidity and more stable secondary structures. Disulfide rich peptides are less prone to enzymatic degradation and can sometimes increase binding affinity to the corresponding receptor.
Conformationally stable disulfide-rich peptides has lead to many selective and potent classes of peptides. Toxin peptides from scorpions (e.g., chlorotoxin), cone snails (e.g., conotoxins), snakes, and spiders as well as host-defense peptides (e.g., α-defensins and β-defensins are important classes with diverse pharmacological applications. Conotoxins and chlorotoxins are potent blockers of ion channels and have been indicated as treatments for chronic pain and cancer.
 

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