Conversion of single-chain or disulfide-bridged dimeric collagenous peptides into Cys(Npys) derivatives as activated species for subsequent regioselective thiol/disulfide exchange reactions leads to side products whose origin and nature was determined by HPLC and ESI-MS. In both cases the high tende
✦ LIBER ✦
A new strategy for regioselective interstrand disulfide bridging of multiple cysteine peptides
✍ Scribed by Johannes Ottl; Luis Moroder
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- French
- Weight
- 257 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0040-4039
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## Abstract The oxidative folding of small, cysteine‐rich peptides to selectively achieve the native disulfide bond connectivities is critical for discovery and structure‐function studies of many bioactive peptides. As the propensity to acquire the native conformation greatly depends on the peptide