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Self-Assembly of Actin Scaffolds at Ponticulin-Containing Supported Phospholipid Bilayers

Benjamin R. G. Johnson ^*, Richard J. Bushby , John Colyer  and Stephen D. Evans ^*

^* School of Physics and Astronomy, and Centre for Self Organising Molecular Systems, University of Leeds, Leeds LS2 9JT, United Kingdom

Correspondence: Address reprint requests and inquiries to Stephen D. Evans, E-mail: s.d.evans{at}leeds.ac.uk.

Phospholipid vesicles containing ponticulin have been used to form solid supported and tethered bilayer lipid membranes. The ponticulin serves as both a nucleation site for actin polymerization as well as a binding site for F-actin. Studies of F-actin binding to such bilayers have demonstrated the formation of an in vitro actin scaffold. The dissociation constant for the binding of F-actin filaments to a ponticulin-containing tethered bilayer was found to be 11 ± 5 nM, indicative of high affinity binding.