Directed formation of lipid membrane microdomains as high affinity sites for His-tagged proteins

J Am Chem Soc. 2009 Jul 1;131(25):8728-9. doi: 10.1021/ja901157c.

Abstract

Lipid membranes composed of an iminodiacetic acid functionalized lipid, DSIDA, in a POPC matrix exhibited switchable properties via Cu(2+) recognition to rapidly assemble microdomains that act as high affinity sites for His-tagged proteins. The microdomains demonstrated an order of magnitude enhanced affinity for the proteins compared to homogeneously functionalized POPC membranes with Ni(2+)-NTA DOGS or Cu(2+)-DOIDA, while a rapid release and restoration of the original membrane was accomplished with micromolar concentrations of EDTA.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Copper / metabolism*
  • Histidine / chemistry
  • Imino Acids / chemistry*
  • Imino Acids / metabolism
  • Lipid Metabolism
  • Lipids / chemistry*
  • Maltose-Binding Proteins
  • Membrane Microdomains / chemistry*
  • Membrane Microdomains / metabolism*
  • Membranes, Artificial
  • Phosphatidylcholines / chemistry
  • Proteins / chemistry
  • Proteins / metabolism*

Substances

  • Carrier Proteins
  • Imino Acids
  • Lipids
  • Maltose-Binding Proteins
  • Membranes, Artificial
  • Phosphatidylcholines
  • Proteins
  • Histidine
  • Copper
  • 1-palmitoyl-2-oleoylphosphatidylcholine
  • iminodiacetic acid