Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins
AU - Abad, J.M.
AU - Mertens, S.F.L.
AU - Pita, M.
AU - Fernández, V.M.
AU - Schiffrin, D.J.
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
KW - Adsorption
KW - Amino acids
KW - Chemical modification
KW - Copper
KW - Enzyme immobilization
KW - Gold
KW - Proteins
KW - Surface treatment
KW - Functionalization
KW - Gold clusters
KW - Histadine-tagged proteins
KW - Thioctic acid-capped gold nanoparticles
KW - Nanostructured materials
KW - cobalt
KW - enzyme
KW - ferredoxin nicotinamide adenine dinucleotide phosphate reductase
KW - gold
KW - histidine
KW - horseradish peroxidase
KW - nanoparticle
KW - thioctic acid
KW - transition element
KW - adsorption
KW - article
KW - genetic engineering
KW - protein binding
KW - protein function
KW - Binding Sites
KW - Cobalt
KW - Enzymes, Immobilized
KW - Ferredoxin-NADP Reductase
KW - Histidine
KW - Horseradish Peroxidase
KW - Ligands
KW - Nanostructures
KW - Spectrophotometry, Ultraviolet
KW - Spectroscopy, Fourier Transform Infrared
KW - Substrate Specificity
KW - Thioctic Acid
KW - Water
U2 - 10.1021/ja042717i
DO - 10.1021/ja042717i
M3 - Journal article
VL - 127
SP - 5689
EP - 5694
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 15
ER -