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. 1994 Feb;66(2 Pt 1):355–359. doi: 10.1016/s0006-3495(94)80784-2

The barrel-stave model as applied to alamethicin and its analogs reevaluated.

D R Laver 1
PMCID: PMC1275702  PMID: 7512830

Abstract

Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The conductance levels have been thought to be due to a barrel-stave structure where conducting pores (barrels) are formed by the self-assembly of a variable number of alpha-helical rods (staves). The conductance transitions were then interpreted as the addition or deletion of peptide monomers from the pore-forming complex (Sansom, M.S. 1991. Prog. Biophys. Mol. Biol. 55:139-235). Initially, pore conductances were calculated from that expected of right circular cylinders of "bulk" electrolyte. More recent theories also included the access resistance of the electrolyte outside the pore. However, they all consistently overestimated the observed conductances. The reason for the discrepancy is presented here. Previous theories ignored the effects of ion concentration gradients near the pore. Hence, they only held in the limit of small bilayer potentials (< 25 mV) and so would overestimate measurements that typically used much larger potentials (> 100 mV). This theoretical flaw is corrected by using Läuger's theory of diffusion-limited ion flow (Läuger, P. 1976. Biochim. Biophys. Acta. 455:493-509). Thus, including the effects of ion concentration gradients results in a considerable improvement in predicting pore conductances. It is found that: 1) the effects of ion concentration gradients must be included in the barrel-stave model for it to apply to the available data; 2) previously published explanations for the discrepancy between the model and the data, namely the "distorted bundle" and the "head-to-tail aggregate" hypotheses are not necessary (reviewed by Sansom, 1991).

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Selected References

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  1. Balaram P., Krishna K., Sukumar M., Mellor I. R., Sansom M. S. The properties of ion channels formed by zervamicins. Eur Biophys J. 1992;21(2):117–128. doi: 10.1007/BF00185426. [DOI] [PubMed] [Google Scholar]
  2. Baumann G., Mueller P. A molecular model of membrane excitability. J Supramol Struct. 1974;2(5-6):538–557. doi: 10.1002/jss.400020504. [DOI] [PubMed] [Google Scholar]
  3. Boheim G. Statistical analysis of alamethicin channels in black lipid membranes. J Membr Biol. 1974;19(3):277–303. doi: 10.1007/BF01869983. [DOI] [PubMed] [Google Scholar]
  4. Gordon L. G., Haydon D. A. Potential-dependent conductances in lipid membranes containing alamethicin. Philos Trans R Soc Lond B Biol Sci. 1975 Jun 10;270(908):433–447. doi: 10.1098/rstb.1975.0021. [DOI] [PubMed] [Google Scholar]
  5. Hall J. E. Access resistance of a small circular pore. J Gen Physiol. 1975 Oct;66(4):531–532. doi: 10.1085/jgp.66.4.531. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hanke W., Boheim G. The lowest conductance state of the alamethicin pore. Biochim Biophys Acta. 1980 Mar 13;596(3):456–462. doi: 10.1016/0005-2736(80)90134-0. [DOI] [PubMed] [Google Scholar]
  7. Levitt D. G. General continuum theory for multiion channel. I. Theory. Biophys J. 1991 Feb;59(2):271–277. doi: 10.1016/S0006-3495(91)82220-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Läuger P. Diffusion-limited ion flow through pores. Biochim Biophys Acta. 1976 Dec 2;455(2):493–509. doi: 10.1016/0005-2736(76)90320-5. [DOI] [PubMed] [Google Scholar]
  9. Menestrina G., Voges K. P., Jung G., Boheim G. Voltage-dependent channel formation by rods of helical polypeptides. J Membr Biol. 1986;93(2):111–132. doi: 10.1007/BF01870804. [DOI] [PubMed] [Google Scholar]
  10. Sansom M. S. Alamethicin and related peptaibols--model ion channels. Eur Biophys J. 1993;22(2):105–124. doi: 10.1007/BF00196915. [DOI] [PubMed] [Google Scholar]
  11. Sansom M. S. The biophysics of peptide models of ion channels. Prog Biophys Mol Biol. 1991;55(3):139–235. doi: 10.1016/0079-6107(91)90004-c. [DOI] [PubMed] [Google Scholar]

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