For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
23
views
104
references
 Top references
cited by
37
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
0 collections
    0
    shares
      283
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Host-Defense Activities of Cyclotides

      review-article
      Author(s):
      Publication date (Electronic):
      Journal: Toxins
      Publisher: MDPI
      Keywords: circular protein, cyclic peptide, cyclotide, cystine knot, insecticide, kalata B1

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Cyclotides are plant mini-proteins whose natural function is thought to be to protect plants from pest or pathogens, particularly insect pests. They are approximately 30 amino acids in size and are characterized by a cyclic peptide backbone and a cystine knot arrangement of three conserved disulfide bonds. This article provides an overview of the reported pesticidal or toxic activities of cyclotides, discusses a possible common mechanism of action involving disruption of biological membranes in pest species, and describes methods that can be used to produce cyclotides for potential applications as novel pesticidal agents.

          Related collections

          Most cited references104

          • Record: found
          • Abstract: found
          • Article: not found

          Synthesis of proteins by native chemical ligation.

          S Kent, P E Dawson, T W Muir … (1994)
          A simple technique has been devised that allows the direct synthesis of native backbone proteins of moderate size. Chemoselective reaction of two unprotected peptide segments gives an initial thioester-linked species. Spontaneous rearrangement of this transient intermediate yields a full-length product with a native peptide bond at the ligation site. The utility of native chemical ligation was demonstrated by the one-step preparation of a cytokine containing multiple disulfides. The polypeptide ligation product was folded and oxidized to form the native disulfide-containing protein molecule. Native chemical ligation is an important step toward the general application of chemistry to proteins.
          Article 0 comments Cited 286 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Total chemical synthesis of proteins.

            Stephen B H Kent (2009)
            This tutorial review outlines the modern ligation methods that enable the efficient total chemical synthesis of enzymes and other protein molecules. Key to this success is the chemoselective reaction of unprotected synthetic peptides ('chemical ligation'). Notably, native chemical ligation enables the reaction of two unprotected peptides in aqueous solution at neutral pH to form a single product in near quantitative yield. Full-length synthetic polypeptides are folded to form the defined tertiary structure of the target protein molecule, which is characterized by mass spectrometry, NMR, and X-ray crystallography, in addition to biochemical and/or biological activity.
            Article 0 comments Cited 168 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.

              D J Craik, N Daly, T. Bond … (1999)
              Several macrocyclic peptides ( approximately 30 amino acids), with diverse biological activities, have been isolated from the Rubiaceae and Violaceae plant families over recent years. We have significantly expanded the range of known macrocyclic peptides with the discovery of 16 novel peptides from extracts of Viola hederaceae, Viola odorata and Oldenlandia affinis. The Viola plants had not previously been examined for these peptides and thus represent novel species in which these unusual macrocyclic peptides are produced. Further, we have determined the three-dimensional structure of one of these novel peptides, cycloviolacin O1, using (1)H NMR spectroscopy. The structure consists of a distorted triple-stranded beta-sheet and a cystine-knot arrangement of the disulfide bonds. This structure is similar to kalata B1 and circulin A, the only two macrocyclic peptides for which a structure was available, suggesting that despite the sequence variation throughout the peptides they form a family in which the overall fold is conserved. We refer to these peptides as the cyclotide family and their embedded topology as the cyclic cystine knot (CCK) motif. The unique cyclic and knotted nature of these molecules makes them a fascinating example of topologically complex proteins. Examination of the sequences reveals they can be separated into two subfamilies, one of which tends to contain a larger number of positively charged residues and has a bracelet-like circularization of the backbone. The second subfamily contains a backbone twist due to a cis-Pro peptide bond and may conceptually be regarded as a molecular Moebius strip. Here we define the structural features of the two apparent subfamilies of the CCK peptides which may be significant for the likely defense related role of these peptides within plants. Copyright 1999 Academic Press.
              Article 0 comments Cited 124 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Journal
                Journal ID (nlm-ta): Toxins (Basel)
                Journal ID (iso-abbrev): Toxins (Basel)
                Journal ID (publisher-id): toxins
                Title: Toxins
                Publisher: MDPI
                ISSN (Electronic): 2072-6651
                Publication date (Electronic): 15 February 2012
                Publication date Collection: February 2012
                Volume: 4
                Issue: 2
                Pages: 139-156
                Affiliations
                Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia; Email: d.craik@ 123456imb.uq.edu.au ; Tel.: +61-7-3346-2019; Fax: +61-7-3346-2101
                Article
                Publisher ID: toxins-04-00139
                DOI: 10.3390/toxins4020139
                PMC ID: 3317112
                PubMed ID: 22474571
                SO-VID: 43175b18-86cc-47bf-8f67-2993ea5faed6
                Copyright © © 2012 by the authors; licensee MDPI, Basel, Switzerland.
                License:

                This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/3.0/).

                History
                Date received : 22 November 2011
                Date revision received : 25 January 2012
                Date accepted : 31 January 2012
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular medicine
                Keywords: circular protein,cyclic peptide,cyclotide,cystine knot,insecticide,kalata b1
                Data availability:
                ScienceOpen disciplines: Molecular medicine
                Keywords: circular protein, cyclic peptide, cyclotide, cystine knot, insecticide, kalata b1

                Comments

                Comment on this article

                scite_

                Similar content283

                See all similar

                Cited by33

                See all cited by

                Most referenced authors751

                See all reference authors