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Cover Picture: A Synthetic Mirror Image of Kalata B1 Reveals that Cyclotide Activity Is Independent of a Protein Receptor (ChemBioChem 16/2011)
Author(s) -
Sando Lillian,
Troeira Henriques Sónia,
Foley Fiona,
Simonsen Shane M.,
Daly Norelle L.,
Hall Kristopher N.,
Gustafson Kirk R.,
Aguilar MarieIsabel,
Craik David J.
Publication year - 2011
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.201190074
Subject(s) - peptide , residue (chemistry) , chemistry , stereochemistry , disulfide bond , receptor , amino acid , cystine , combinatorial chemistry , biochemistry , cysteine , enzyme
The cover picture shows mirror image forms of the cyclotide kalata B1, a 29‐residue peptide with a cyclic backbone and a cystine knot. The native peptide is isolated from the African plant Oldenlandia affinis , which is used in an indigenous medicinal tea to accelerate labour, but has a range of other activities, including anti‐HIV activity. The synthetic mirror image form, made from D ‐amino acids, was assembled by solid‐phase peptide synthesis and used to demonstrate that membrane binding, rather than a chiral receptor, is implicated in cyclotide bioactivity. For more information, see the paper by D. J. Craik et al. on p. 2456 ff. (Cover art designed by David Wilson, University of Queensland.)