Peptaibols are membrane-active polypeptides isolated from fungal sources. They are characterized by the presence of an unusual amino acid, α-aminoisobutyric acid, and a C-terminal hydroxylated amino acid. Peptaibols exhibit antibiotic activity against bacteria and fungi. Their amphipathic nature allows them to self-associate into oligomeric ion-channel assemblies which span the width of lipid bilayer membranes. Over 200 peptaibol sequences have been reported to date, which are compiled in the Peptaibol Database at http://www.cryst.bbk.ac.uk/peptaibol. Alignments of these sequences have been carried out in order to define a series of related subfamilies (SFs) with common sequence features thought to be important for channel formation. Crystal structures determined for a number of peptaibols from the various SFs provide the bases both for modelling of the channel structures and for modelling structures of other members of the same SFs.
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Conference Article|
August 01 2001
Peptaibols: models for ion channels
J. K. Chugh;
J. K. Chugh
1Department of Crystallography, Birkbeck College, University of London, London WCIE 7HX, U.K.
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B. A. Wallace
B. A. Wallace
1
1Department of Crystallography, Birkbeck College, University of London, London WCIE 7HX, U.K.
1To whom correspondence should be addressed (e-mail ubcg25a@mail.cryst.bbk.ac.uk)
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Publisher: Portland Press Ltd
Received:
February 20 2001
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2001 Biochemical Society
2001
Biochem Soc Trans (2001) 29 (4): 565–570.
Article history
Received:
February 20 2001
Citation
J. K. Chugh, B. A. Wallace; Peptaibols: models for ion channels. Biochem Soc Trans 1 August 2001; 29 (4): 565–570. doi: https://doi.org/10.1042/bst0290565
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