FEBS Letters
Volume 583, Issue 14 , Pages 2321-2325, 21 July 2009

Electric dipole reorientation in the interaction of botulinum neurotoxins with neuronal membranes

Edited by Maurice Montal

  • Federico Fogolari

      Affiliations

    • Department of Biomedical Sciences and Technologies, University of Udine, Piazzale Kolbe 4, 33100 Udine, Italy
    • These authors equally contributed to this work.
  • ,
  • Silvio C.E. Tosatto

      Affiliations

    • Department of Biology, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy
    • These authors equally contributed to this work.
  • ,
  • Lucia Muraro

      Affiliations

    • Department of Biomedical Sciences, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy
  • ,
  • Cesare Montecucco

      Affiliations

    • Department of Biomedical Sciences, University of Padua, Viale G. Colombo 3, 35121 Padua, Italy
    • Corresponding Author InformationCorresponding author. Fax: +39 49 827 60 49.

Received 22 May 2009; received in revised form 25 June 2009; accepted 28 June 2009. published online 02 July 2009.

Abstract 

Botulinum neurotoxins are highly potent toxins capable of rapid and specific interaction with the presynaptic membrane. We have hypothesised that: (1) these neurotoxins possess an electric dipole with the positive pole on receptor binding domain Hc-C and that (2) on approaching the negatively charged presynaptic membrane, they reorient themselves and hit the membrane surface with Hc-C; this electrostatic effect would contribute efficient binding. Electrostatic calculations confirm these hypotheses and strongly indicate that electrostatics effects can play an important role in the unique presynaptic membrane binding properties of these neurotoxins and generally on the interaction of other plasma membrane protein ligands.

Abbreviations: BoNT, botulinum neurotoxin, SV, synaptic vesicle

Keywords: Botulinum neurotoxin, Membrane electrostatics, Protein dipole, Presynaptic membrane

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PII: S0014-5793(09)00509-2

doi:10.1016/j.febslet.2009.06.046

FEBS Letters
Volume 583, Issue 14 , Pages 2321-2325, 21 July 2009