The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers.

Abstract

The heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayer membranes. Channel activity is confined to the N-terminal half of this chain; the C-terminal half is inactive. Channel activity is stimulated by low pH (4.5-5.5) on the cis side (the side to which protein is added), neutral pH on the opposite (trans) side, and cis positive voltages. These findings are strikingly similar to those previously reported for analogous fragments of diphtheria and tetanus toxins.

• Authors: R O Blaustein, W J Germann, A Finkelstein, B R DasGupta
• Journal: FEBS letters (FEBS Lett) Vol. 226 Issue 1 Pg. 115-20 (Dec 21 1987) ISSN: 0014-5793 [Print] England
• PMID: 2446925 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Ion Channels
• Lipid Bilayers
• Macromolecular Substances
• Neurotoxins
• Phosphatidylcholines
• Phosphatidylethanolamines
• Phosphatidylserines
• Botulinum Toxins

Topics

• Botulinum Toxins
• Hydrogen-Ion Concentration
• Ion Channels (physiology)
• Lipid Bilayers
• Macromolecular Substances
• Models, Biological
• Molecular Weight
• Neurotoxins
• Phosphatidylcholines
• Phosphatidylethanolamines
• Phosphatidylserines