Capped acyclic permutants of the circular protein kalata B1
- 27 October 2004
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 577 (3) , 399-402
- https://doi.org/10.1016/j.febslet.2004.10.034
Abstract
The cyclotides are a family of head-to-tail cyclized peptides that display exceptionally high stability and a range of biological activities. Acyclic permutants that contain a break in the circular backbone have been reported to be devoid of the haemolytic activity of the prototypic cyclotide kalata B1, but the potential role of the charges at the introduced termini in this loss of membraneolytic activity has not been fully determined. In this study, acyclic permutants of kalata B1 with capped N- and C-termini were synthesized and found to adopt a native fold. These variants were observed to cause no measurable lysis of erythrocytes, strengthening the connection between backbone cyclization and haemolytic activityKeywords
This publication has 13 references indexed in Scilit:
- A Comparison of the Self-association Behavior of the Plant Cyclotides Kalata B1 and Kalata B2 via Analytical UltracentrifugationJournal of Biological Chemistry, 2004
- Linearization of a Naturally Occurring Circular Protein Maintains Structure but Eliminates Hemolytic Activity,Biochemistry, 2003
- Twists, Knots, and Rings in ProteinsJournal of Biological Chemistry, 2003
- Biosynthesis and insecticidal properties of plant cyclotides: The cyclic knotted proteins from Oldenlandia affinisProceedings of the National Academy of Sciences, 2001
- Acyclic Permutants of Naturally Occurring Cyclic ProteinsJournal of Biological Chemistry, 2000
- New Circulin Macrocyclic Polypeptides from Chassalia parvifoliaJournal of Natural Products, 2000
- Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motifJournal of Molecular Biology, 1999
- Elucidation of the Primary and Three-Dimensional Structure of the Uterotonic Polypeptide Kalata B1Biochemistry, 1995
- Cyclopsychotride A, a Biologically Active, 31-Residue Cyclic Peptide Isolated from Psychotria longipesJournal of Natural Products, 1994
- A common structural motif incorporating a cystine knot and a triple‐stranded β‐sheet in toxic and inhibitory polypeptidesProtein Science, 1994