American Chemical Society, Journal of the American Chemical Society, 15(127), p. 5689-5694, 2005
DOI: 10.1021/ja042717i
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This paper presents an efficient strategy for the specific immobilization of fully functional proteins onto the surface of nanoparticles. Thioctic acid-derivatized gold clusters are used as a scaffold for further stepwise modification, leading to a cobalt(II)-terminated ligand shell. A histidine tag introduced by genetic engineering into a protein is coordinated to this transition metal ion. The specific immobilization has been demonstrated for the cases of a genetically engineered horseradish peroxidase and ferredoxin-NADP(+) reductase, confirming the attachment of the fully functional proteins to the Co(II)-terminated nanointerface. The absence of nonspecific protein adsorption and the specificity of the binding site have been verified using several analogues of the enzymes without the histidine tag.