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Published July 1994 | public
Journal Article

Specific Protein Attachment to Artificial Membranes via Coordination to Lipid-Bound Copper(II)


A versatile and convenient method for targeting proteins to lipid assemblies using metal ion coordination is described. Mixed lipid bilayers and Langmuir monolayers containing a metal-chelating lipid and divalent copper ions are shown to bind protein via surface-accessible histidine residues. Cu^(2+) chelated by iminodiacetate (IDA) in the headgroup serves as an affinity ligand to target the protein to the interface. The compact, uncharged Cu^(2+)-IDA headgroup can be incorporated into lipid assemblies without disrupting the lipid packing. Surface pressure-area isotherms of DSPC monolayers containing 5 mol % of IDA-lipid show that Cu^(2+) enhances the rate and extent of myoglobin association with the interface. Myoglobin binds to small unilamellar vesicles containing 2% Cu^(2+)-IDA lipid (48% DSPC and 50% cholesterol) at least an order of magnitude more tightly than to vesicles without metal or loaded with Ca^(2+). The Cu^(2+)-IDA lipid more than doubles the amount of protein targeted to the interface. Cu^(2+) ESR parameters g_∥ and A_∥, measured for liposomes with native and DEPC-modified myoglobin, support coordination of surface histidine side chains to Cu^(2+) as the binding interaction.

Additional Information

© 1994 American Chemical Society. Received February 17, 1994. In Final Form: April 11, 1994. This research is supported by the Office of Naval Research (N00014-92-J-1178) and the National Science Foundation (BCS-9108502). F.H.A. acknowledges an NSF PYI award and a fellowship from the David and Lucile Packard Foundation. D.R.S. is supported by a predoctoral training fellowship from the National Institute of General Medical Sciences, Pharmacology Sciences Program. D.W.P. is a Landau Fellow.

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