Dissecting the oxidative folding of circular cystine knot miniproteins

Gunasekera, Sunithi, Daly, Norelle L., Clark, Richard J. and Craik, David J. (2009) Dissecting the oxidative folding of circular cystine knot miniproteins. Antioxidants and Redox Signalling, 11 5: 971-980. doi:10.1089/ars.2008.2295

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ181281_fulltext.pdf Full text (open access) application/pdf 452.85KB 0

Author Gunasekera, Sunithi
Daly, Norelle L.
Clark, Richard J.
Craik, David J.
Title Dissecting the oxidative folding of circular cystine knot miniproteins
Journal name Antioxidants and Redox Signalling   Check publisher's open access policy
ISSN 1523-0864
Publication date 2009-05-01
Year available 2009
Sub-type Article (original research)
DOI 10.1089/ars.2008.2295
Open Access Status File (Author Post-print)
Volume 11
Issue 5
Start page 971
End page 980
Total pages 10
Editor Chandan K. Sen
Dipak K. Das
Place of publication Larchmont, NY, United States of America
Publisher Mary Ann Liebert
Language eng
Subject C1
970106 Expanding Knowledge in the Biological Sciences
0601 Biochemistry and Cell Biology
060112 Structural Biology (incl. Macromolecular Modelling)
Abstract Cyclotides are plant proteins with exceptional stability owing to the presence of a cyclic backbone and three disulfide bonds arranged in a cystine knot motif. Accordingly, they have been proposed as templates to stabilize bioactive epitopes in drug-design applications. The two main subfamilies, referred to as the Möbius and bracelet cyclotides, require dramatically different in vitro folding conditions to achieve the native fold. To determine the underlying elements that influence cyclotide folding, we examined the in vitro folding of a suite of hybrid cyclotides based on combination of the Möbius cyclotide kalata B1 and the bracelet cyclotide cycloviolacin O1. The folding pathways of the two cyclotide subfamilies were found to be different and influenced by specific residues within intercysteine loops 2 and 6. Two changes in these loops, a substitution in loop 2 and an addition in loop 6, enabled the folding of a cycloviolacin O1 analogue under conditions in which folding does not occur in vitro for the native peptide. A key intermediate contains a native-like hairpin structure that appears to be a nucleation locus early in the folding process. Overall, these mechanistic findings on the folding of cyclotides are potentially valuable for the design of new drug leads. Copyright Mary Ann Liebert, Inc.
Keyword Cyclotide Cycloviolacin O2
Q-Index Code C1
Q-Index Status Confirmed Code
Additional Notes This is a copy of an article published in Antioxidants and Redox Signalling ©2009 copyright Mary Ann Liebert, Inc.; Antioxidants and Redox Signalling is available online at: http://online.liebertpub.com

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2010 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 26 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 29 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Thu, 03 Sep 2009, 18:23:04 EST by Mr Andrew Martlew on behalf of Institute for Molecular Bioscience