The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide

C. F. Snook, G. A. Woolley, G. Oliva, Vasantha Pattabhi, Stephen Paul Wood, T. L. Blundell, B. A. Wallace

Research output: Contribution to journalArticlepeer-review


BACKGROUND: Antiamoebin is a member of the peptaibol family of polypeptides and has a unique antibiotic activity: it acts as an antiamoebic agent, but does not effectively haemolyze erythrocytes even though it does exhibit membrane-modifying activity.

RESULTS: The structure of antiamoebin I has been determined by X-ray crystallography at 1.4 A resolution. The molecule forms a helical structure, which, as a result of the presence of a number of proline and hydroxyproline residues, has a deep bend in the middle. Circular dichroism spectroscopy, single-channel conductance studies and fluorescence diffusion studies suggest a mode of ion transport that is entirely different from that of the other two members of the peptaibol family (alamethicin and zervamicin) whose structures and functions have been examined in detail.

CONCLUSIONS: The structure of the polypeptide has been determined and a functional model for its mode of action in membranes is presented. Although under some conditions antiamoebin may form ion channels, unlike the closely related alamethicin and zervamicin polypeptides, its major membrane-modifying activity appears to be as an ion carrier.
Original languageEnglish
Pages (from-to)783-792
Issue number6
Publication statusPublished - 1 Jun 1998


  • circular dichroism spectroscopy
  • conductance
  • crystal structure
  • ion channels
  • membrane transport


Dive into the research topics of 'The structure and function of antiamoebin I, a proline-rich membrane-active polypeptide'. Together they form a unique fingerprint.

Cite this