Directed formation of lipid membrane microdomains as high affinity sites for His-tagged proteins.
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.
Hayden
Carl C
CC
Sandia National Laboratories, P.O. Box 969, Livermore, California 94551, USA.
Hwang
Jane S
JS
Abate
Elisa A
EA
Kent
Michael S
MS
Sasaki
Darryl Y
DY
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism; D003300:Copper / Q000378:metabolism*; D006639:Histidine / Q000737:chemistry; D007098:Imino Acids / Q000737:chemistry* / Q000378:metabolism; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D058619:Maltose-Binding Proteins; D021962:Membrane Microdomains / Q000737:chemistry* / Q000378:metabolism*; D008567:Membranes, Artificial; D010713:Phosphatidylcholines / Q000737:chemistry; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D002352:Carrier Proteins; D007098:Imino Acids; D008055:Lipids; D058619:Maltose-Binding Proteins; D008567:Membranes, Artificial; D010713:Phosphatidylcholines; D011506:Proteins; D006639:Histidine; D003300:Copper; C028694:1-palmitoyl-2-oleoylphosphatidylcholine; C008109:iminodiacetic acid