Author(s): Abad JM, Mertens SF, Pita M, Fernndez VM, Schiffrin DJ
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Abstract 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.
This article was published in J Am Chem Soc
and referenced in Journal of Biosensors & Bioelectronics