Abstracts of oral presentations

• Publisher: Wiley (John Wiley & Sons)
• Year: 2005
• Tongue: English
• Weight: 126 KB
• Volume: 80
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.20321

✦ Synopsis

The right 3D-conformation of a peptide, is essential for its biological activity. Nature has found many elegant ways to reduce the flexibility of peptides/proteins in order to control their folding and shape for increasing affinity as well as selectivity for receptor interaction. Disulfide bridges, thioether bridges and the even more sophisticated multiple side chain knotting, are well-known ways to control the 3D-shape. Outstanding examples in this respect are the peptide antibiotics vancomycin (having multiple side chain knotting) and nisin Z (containing e.g. a crossed bisthioether ring system). Inspired by vancomycin we describe here the synthesis of cyclic tripeptides and bicyclic pentapeptides with an alkyne/alkene moiety as part of the cyclic constraint, using Sonogashira-, Heck-and ring-closing metathesis reactions [1]. Furthermore, the synthesis of a crossed alkene-bridged mimic of the nisin Z bisthioether ring system will be presented. This ring system could be synthesized in a single metathesis reaction step and the correct side chain connectivities may imply a considerable degree of preorganization of the linear metathesis precursor [2]. In addition, recent results using ring-closing alkyne metathesis on pentapeptides followed by stereoselective reduction of the triple bond will be discussed.