title: Direct observation of counterion organization in F-actin polyelectrolyte bundles.
abstract: Attractions between like-charged polyelectrolytes have been observed in a variety of systems (W.M. Gelbart, R.F. Bruinsma, P.A. Pincus, V.A. Parsegian, Phys. Today 53, September issue, 38 (2000)). Recent biological examples include DNA, filamentous viruses, and F-actin. Theoretical investigations on idealized systems indicate that counterion correlations play a central role, but no experiments that specifically probe such correlations have been performed. Using synchrotron X-ray diffraction, we have directly observed the organization of multivalent ions on cytoskeletal filamentous actin (a well-defined biological polyelectrolyte) and found an unanticipated symmetry-breaking collective counterion mechanism for generating attractions. Surprisingly, the counterions do not form a lattice that simply follows actin's helical symmetry; rather, the counterions organize into "frozen" ripples parallel to the actin filaments and form structures reminiscent of charge density waves. Moreover, these 1D counterion charge density waves form a coupled mode with twist deformations of the oppositely charged actin filaments. This counterion organization is not sensitive to thermal fluctuations in temperature range accessible to protein-based polyelectrolyte systems. Moreover, the counterion density waves are "pinned" to the spatial periodicity of charges on the actin filament even if the global filament charge density is varied, indicating the importance of charge periodicity on the polyelectrolyte substrate.
authors.affiliation: Department of Materials Science & Engineering, University of Illinois at Urbana-Champaign, IL 61801, USA.
authors.forename: T E
authors.initials: TE
authors.lastname: Angelini
authors.forename: H
authors.initials: H
authors.lastname: Liang
authors.forename: W
authors.initials: W
authors.lastname: Wriggers
authors.forename: G C L
authors.initials: GC
authors.lastname: Wong
mesh_terms: D008841:Actin Cytoskeleton / Q000187:drug effects / Q000378:metabolism; D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism / Q000494:pharmacology; D003432:Cross-Linking Reagents / Q000378:metabolism / Q000494:pharmacology; D004573:Electrolytes / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism / Q000494:pharmacology; D008840:Microfilament Proteins / Q000378:metabolism; D011817:Rabbits; D053838:Scattering, Small Angle; D017356:Synchrotrons; D013816:Thermodynamics; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D003432:Cross-Linking Reagents; D004573:Electrolytes; D008840:Microfilament Proteins; D008274:Magnesium; D002118:Calcium