Coupling artificial actin cortices to biofunctionalized lipid monolayers

Kheya Sengupta, Laurent Limozin, Matthias Tristl, Ilka Haase, Markus Fischer, Erich Sackmann

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

We report the assembly of protein supramolecular structures at an air-water interface and coupling of artificial actin cortices to such structures. The coupling strategies adopted include electrostatic binding of actin to monolayers doped with lipids, exposing positively charged poly(ethylene glycol) headgroups; binding of biotinylated actin to lipids carrying biotin headgroups through avidin; binding of actin to membranes through biotinylated hisactophilin (a cellular actin-membrane coupler) using an avidin-biotin linkage; and coupling of actin to membranes carrying chelating lipids through a 15-nm-diameter protein capsid (bacterial lumazine synthase or LuSy) exhibiting histidine tags (which bind both to actin and to the chelating lipid). The distribution of the proteins in a direction normal to the interface was measured by neutron reflectivity under different conditions of pH and ionic strength. In the case of the first three binding methods, the thickness of the actin film was found to correspond to a single actin filament. Multilayers of actin could be formed only by using the multifunctional LuSy couplers that exhibit 60 hexahistidine tags and can thus act as actin cross-linkers. The LuSy-mediated binding can be reversibly switched by pH variations,

Original languageEnglish
Pages (from-to)5776-5785
Number of pages10
JournalLangmuir
Volume22
Issue number13
DOIs
StatePublished - 20 Jun 2006

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