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Structure of circulin B and implications for antimicrobial activity of the cyclotides

  1. Author:
    Koltay, A.
    Daly, N. L.
    Gustafson, K. R.
    Craik, D. J.

  2. Author Address

    Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia. NCI, Mol Targets Dev Program, Ctr Canc Res, Frederick, MD 21701 USA Craik, DJ, Univ Queensland, Inst Mol Biosci, Brisbane, Qld 4072, Australia
    1. Year: 2005
    2. Date: MAR
  2. Journal: International Journal of Peptide Research and Therapeutics
    1. 11
    2. 1
    3. Pages: 99-106
  4. Type of Article: Article
  1. Abstract:

    The solution structure of one of the first members of the cyclotide family of macrocyclic peptides to be discovered, circulin B has been determined and compared with that of circulin A and related cyclotides. Cyclotides are mini-proteins derived from plants that have the characteristic features of a head-to-tail cyclised peptide backbone and a knotted arrangement of their three disulfide bonds. First discovered because of their uterotonic or anti-HIV activity, they have also been reported to have activity against a range of Gram positive and Gram negative bacteria as well as fungi. The aim of the current study was to develop structure-activity relationships to rationalise this antimicrobial activity. Comparison of cyclotide structures and activities suggests that the presence and location of cationic residues may be a requirement for activity against Gram negative bacteria. Understanding the topological differences associated with the antimicrobial activity of the cyclotides is of significant interest and potentially may be harnessed for pharmaceutical applications

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External Sources

  1. View record in Web of Science®
  2. WOS: 000229632900007

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