PMID: 7540870Jun 14, 1995Paper

Ion channel formation by synthetic analogues of staphylococcal delta-toxin

Biochimica Et Biophysica Acta
I D KerrM S Sansom

Abstract

Ion channel formation by three analogues of staphylococcal delta-toxin, an amphipathic and alpha-helical channel-forming peptide, has been evaluated by measurement of ionic currents across planar lipid bilayers. Replacement of beta-branched, hydrophobic residues by leucine and movement of a tryptophan residue from the hydrophilic to the hydrophobic face of the helix does not significantly alter ion channel activity. Removal of the N-terminal blocking group combined with the substitution of glycine-10 by leucine changes the single channel properties of delta-toxin, without altering macroscopic conductance/voltage behaviour. Truncation of the N-terminus by three residues results in complete loss of channel-forming activity. These changes in channel-forming properties upon altering the peptide sequence do not mirror changes in haemolytic activity. The results lend support to the proposal that channel formation and haemolysis are distinct events. Channel properties are discussed in the context of a model in which the pore is formed by a bundle of approximately parallel transbilayer helices.

References

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Citations

Oct 12, 2001·Toxicon : Official Journal of the International Society on Toxinology·C L Sears
Apr 30, 2003·Proceedings of the National Academy of Sciences of the United States of America·Davor PavlovićNicole Zitzmann
Mar 17, 1999·The Journal of Experimental Medicine·C MehlinS J Klebanoff
Oct 21, 1999·Microbiology and Immunology·M MuraiS Masuda
Aug 26, 2003·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·E F SchwartzL C Salomão
Mar 1, 1996·Microbiological Reviews·C L Sears, J B Kaper
Mar 1, 1997·Infection and Immunity·A A FrancoC L Sears

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