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Cover Picture: NMR as an Effective Tool for the Structure Determination of Lasso Peptides (ChemBioChem 5/2012)
The cover picture shows a 3D structure and orthogonal views of capistruin, a highly stable lasso peptide produced by Burkholderia thailandensis. Lasso peptides are a class of ribosomally assembled natural products of bacterial origin. They feature a side-chain-to-backbone macrolactam ring through which eight or nine residues of the C-terminal part of the sequence are threaded. In the Minireview by M. A. Marahiel and X. Xie on p. 621 ff., the characteristic structural features of lasso peptides and the NMR spectroscopy methods used to define them are presented. The lasso structure was discovered 20 years ago, and nine structures have been published. Their compact fold makes lasso peptides highly stable against proteolytic degradation. This feature and their common biological activity as enzyme inhibitors suggest them to be interesting candidates for drug design. The cover picture was designed by Julian Hegemann (Philipps University Marburg).