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Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins

Research output: Contribution to Journal/MagazineJournal articlepeer-review

<mark>Journal publication date</mark>2005
<mark>Journal</mark>Journal of the American Chemical Society
Issue number15
Number of pages6
Pages (from-to)5689-5694
Publication StatusPublished
<mark>Original language</mark>English


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. © 2005 American Chemical Society.