Pseudo-prolines in cyclic peptides: Conformational stabilisation of cyclo[Pro-Thr(ψMe,Mepro)-Pro]
✍ Scribed by Thomas Rückle; Pierre de Lavallaz; Michael Keller; Pascal Dumy; Manfred Mutter
- Book ID
- 104209586
- Publisher
- Elsevier Science
- Year
- 1999
- Tongue
- French
- Weight
- 382 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0040-4020
No coin nor oath required. For personal study only.
✦ Synopsis
Linear peptide H-Pro-Thr(WM~MCpro)-Pro-OH containing a preformed c/s-Pro-Thr(W~c'MCpro) tertiary amide bond cyclises instantaneously and free of formation of oligomeric structures to the cyclic tripeptide cyclo-[Pro-Thr(WM~MCpro)-Pro]. Even at concentrations up to 10 "1 M peptide, no oligomeric structures are detected by mass spectroscopy and HPLC. 2D IH NMR studies of purified cycintripeptide reveal the compound to exist in one single conformation with all peptide bonds in the c/s conformation. These results indicate enhanced cyclisation tendencies of cis-amide bond containing peptides of short chain length.