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Cover Picture: Ultra‐Stable Peptide Scaffolds for Protein Engineering—Synthesis and Folding of the Circular Cystine Knotted Cyclotide Cycloviolacin O2 (ChemBioChem 1/2008)
Author(s) -
Leta Aboye Teshome,
Clark Richard J.,
Craik David J.,
Göransson Ulf
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200790068
Subject(s) - peptide , chemistry , cyclic peptide , polyproline helix , protein folding , structural motif , protein engineering , stereochemistry , disulfide bond , folding (dsp implementation) , combinatorial chemistry , biochemistry , enzyme , electrical engineering , engineering
The cover picture shows the protected linear peptide precursor and a schematic representation of the folding that leads to the native structure of the cyclotide cycloviolacin O2. This peptide was first isolated from the sweet violet, Viola odorata , which is shown in the background. The cyclotide peptide family defines the cyclic cystine knot motif, which arises from a seamless peptide backbone and the knotted arrangement of three disulfide bonds. This motif is a prime target for protein engineering due to its inherent stability and structural plasticity. However, synthesis and folding of members of the most diverse and biologically active cyclotide subfamily, the bracelets, has been a big challenge. The article by U. Göransson et al. on p. 103 ff. describes the key solution to these problems and thus provides an efficient method of exploring the most potent cyclic cystine knot peptides.