Discovery, structure and biological activities of the cyclotides

Craik, D. J., Daly, N. L., Mulvenna, J., Plan, M. R. and Trabi, M. (2004) Discovery, structure and biological activities of the cyclotides. Current Protein & Peptide Science, 5 5: 297-315. doi:10.2174/1389203043379512


Author Craik, D. J.
Daly, N. L.
Mulvenna, J.
Plan, M. R.
Trabi, M.
Title Discovery, structure and biological activities of the cyclotides
Journal name Current Protein & Peptide Science   Check publisher's open access policy
ISSN 1389-2037
Publication date 2004
Sub-type Critical review of research, literature review, critical commentary
DOI 10.2174/1389203043379512
Volume 5
Issue 5
Start page 297
End page 315
Total pages 19
Place of publication Hilversum
Publisher Bentham Science Publ Ltd
Collection year 2004
Language eng
Subject C1
250302 Biological and Medical Chemistry
780105 Biological sciences
Abstract The cyclotides are a family of small disulfide rich proteins that have a cyclic peptide backbone and a cystine knot formed by three conserved disulfide bonds. The combination of these two structural motifs contributes to the exceptional chemical, thermal and enzymatic stability of the cyclotides, which retain bioactivity after boiling. They were initially discovered based on native medicine or screening studies associated with some of their various activities, which include uterotonic action, anti-HIV activity, neurotensin antagonism, and cytotoxicity. They are present in plants from the Rubiaceae, Violaceae and Cucurbitaccae families and their natural function in plants appears to be in host defense: they have potent activity against certain insect pests and they also have antimicrobial activity. There are currently around 50 published sequences of cyclotides and their rate of discovery has been increasing over recent years. Ultimately the family may comprise thousands of members. This article describes the background to the discovery of the cyclotides, their structural characterization, chemical synthesis, genetic origin, biological activities and potential applications in the pharmaceutical and agricultural industries. Their unique topological features make them interesting from a protein folding perspective. Because of their highly stable peptide framework they might make useful templates in drug design programs, and their insecticidal activity opens the possibility of applications in crop protection.
Keyword Biochemistry & Molecular Biology
Polypeptide Kalata B1
Cystine Knot Motif
Oldenlandia-affinis
Plant Cyclotides
Macrocyclic Peptides
Circular Proteins
Trypsin-inhibitor
Beta-sheet
Momordica-cochinchinensis
Asparaginyl Endopeptidase
Q-Index Code C1

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
2005 Higher Education Research Data Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 15 Aug 2007, 04:38:28 EST