Peptaibols: models for ion channels

Peptaibols are membrane-active polypeptides isolated from fungal sources. They are characterized by the presence of an unusual amino acid, alpha-aminoisobutyric acid, and a C-terminal hydroxylated amino acid. Peptaibols exhibit antibiotic activity against bacteria and fungi. Their amphipathic nature...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 29; no. Pt 4; p. 565
Main Authors Chugh, J K, Wallace, B A
Format Journal Article
LanguageEnglish
Published England 01.08.2001
Subjects
Alamethicin - chemistry
Amino Acid Sequence
Anti-Bacterial Agents - chemistry
Conserved Sequence
Crystallography, X-Ray
Ion Channels - chemistry
Models, Biological
Peptaibols
Peptides
Sequence Alignment
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Summary:Peptaibols are membrane-active polypeptides isolated from fungal sources. They are characterized by the presence of an unusual amino acid, alpha-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.
ISSN:0300-5127
DOI:10.1042/bst0290565