Analysis of peptaibol sequence composition: implications for in vivo synthesis and channel formation

  title={Analysis of peptaibol sequence composition: implications for in vivo synthesis and channel formation},
  author={Lee Whitmore and B. A. Wallace},
  journal={European Biophysics Journal},
The sequence entries in the Peptaibol Database were analysed to provide information on compositional features of this unusual family of peptides. The non-standard amino acid α-aminoisobutyric acid represents almost 40% of the residues in all the known sequences. Glutamine is the only significant polar residue in peptaibols, and the position and number of these residues appear to be related to their functional properties as ion channels. Aromatic residues are clustered at the termini, which may… 

Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin

This short review compares the monomeric structures of three selected peptaibols that widely differ with regards to their near-central kink angles and dipolar moment orientations and shows these structural features to be correlated to the different patterns of channel activity, both at the macroscopic and single-channel levels of investigation.

The Peptaibol Database: a database for sequences and structures of naturally occurring peptaibols

The Peptaibol Database is a sequence and structure resource for the unusual class of peptides known as peptaibols. These peptides exhibit antibiotic and membrane channel-forming activities. The

Biosynthesis and Molecular Genetics of Peptaibiotics—Fungal Peptides Containing Alpha, Alpha-Dialkyl Amino Acids

This work has shown that microheterogeneous peptaibiotics are synthesized by nonribosomal peptide synthetases (NRPSs) via the multiple-carrier thiotemplate mechanism and that still much needs to be learned about substrate selectivity and the regulation of peptibiotics biosynthesis.

Systematic Design and Validation of Ion Channel Stabilization of Amphipathic α-Helical Peptides Incorporating Tryptophan Residues

The ion channel forming capability of a series of peptides showed that the cation−π interactions between Trp and Lys residues in adjacent transmembrane helices contribute to remarkable stabilization of the channel structure.

Isovaline in naturally occurring peptides: A nondestructive methodology for configurational assignment.

The recently developed (1)H-NMR method, which enables the nondestructive assignment of the configuration of each Iva residue in a peptide of known helical screw sense, was applied and proved to be generally applicable and provided evidence that, in the peptaibiotic bergofungin A, the Iva(12) configuration is (R) and not (S) as reported previously.

Peptaibiomics: an advanced, rapid and selective analysis of peptaibiotics/peptaibols by SPE/LC-ES-MS

A specific and rapid screening method applicable directly onto filamentous fungi cultured in a single Petri dish and the judgement is possible whether or not structures are novel, already known or related to known structures.

Facts and Challenges in the Understanding of the Biosynthesis of Peptaibols by Trichoderma

This review article used the recent knowledge on biosynthesis and production of these components to speculate on some of the unknown points and highlights areas where further research is most urgently needed.

Cyclodextrin-scaffolded alamethicin with remarkably efficient membrane permeabilizing properties and membrane current conductance.

Alamethicin belongs to a class of peptides called peptaibols and represents one of these antimicrobial peptides, and the α-helices of the templated multimers were demonstrated to insert into lipid bilayers forming highly efficient and remarkably stable ion-channels.



Peptaibols: models for ion channels.

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.

Solution NMR studies of antiamoebin, a membrane channel-forming polypeptide.

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

The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles.

The bend structure observed for chrysospermin C is compatible with the sequences of all 18 long peptaibols and may represent a common 'active' conformation, which would be appropriate for the formation of oligomeric ion channels.

Alamethicin and related peptaibols — model ion channels

  • M. Sansom
  • Biology
    European Biophysics Journal
  • 2004
These studies suggest that peptaibols form proline-kinked α-helices, and that there may be “hinge-bending” movement of the helix in the region of the central proline residue.

Crystal structure of the channel-forming polypeptide antiamoebin in a membrane-mimetic environment.

Crystals of an ion-channel-forming peptaibol peptide in a partial membrane environment have been obtained by cocrystallizing antiamoebin with n-octanol. The antiamoebin molecule has a bent helical

The stereochemistry of peptides containing alpha-aminoisobutyric acid.

Crystal structures of over three dozen Aib-containing peptides, ranging in length from 2 to 11 residues, have been reported so far which exemplify various types of beta-turns, consecutive beta- turns, and helical structures.

Tryptophans in membrane proteins. X-ray crystallographic analyses.

The tryptophan locations with respect to the lipid bilayer are strikingly non-uniform in nearly all of the membrane proteins examined, providing evidence for possible structural roles fortryptophans in transmembrane sheets and helices, where they may play a part in the stabilization of the trans Membrane segments and perhaps in the orientation and bilayer insertion processes.

Crystal structure of [Leu1]zervamicin, a membrane ion-channel peptide: implications for gating mechanisms.

Structures in four different crystal forms of [Leu1]zervamicin, a membrane channel-forming polypeptide from Emericellopsis salmosynnemata, have been determined by x-ray diffraction, suggesting a gating mechanism for cation transport.

Effect of Nα-Acyl Chain Length on the Membrane-Modifying Properties of Synthetic Analogs of the Lipopeptaibol Trichogin GA IV

Trichogin GA IV, an 11-residue lipopeptaibol blocked at the N-terminus by an n-octanoyl group and at the C-terminus by a 1,2-amino alcohol (l-leucinol), extracted from the fungus Trichoderma