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
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism
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Copper / metabolism*
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Histidine / chemistry
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Imino Acids / chemistry*
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Imino Acids / metabolism
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Lipid Metabolism
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Lipids / chemistry*
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Maltose-Binding Proteins
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Membrane Microdomains / chemistry*
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Membrane Microdomains / metabolism*
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Membranes, Artificial
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Phosphatidylcholines / chemistry
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Proteins / chemistry
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Proteins / metabolism*
Substances
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Carrier Proteins
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Imino Acids
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Lipids
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Maltose-Binding Proteins
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Membranes, Artificial
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Phosphatidylcholines
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Proteins
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Histidine
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Copper
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1-palmitoyl-2-oleoylphosphatidylcholine
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iminodiacetic acid