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

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Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins. / Abad, J.M.; Mertens, S.F.L.; Pita, M.; Fernández, V.M.; Schiffrin, D.J.

In: Journal of the American Chemical Society, Vol. 127, No. 15, 2005, p. 5689-5694.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Abad, JM, Mertens, SFL, Pita, M, Fernández, VM & Schiffrin, DJ 2005, 'Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins', Journal of the American Chemical Society, vol. 127, no. 15, pp. 5689-5694. https://doi.org/10.1021/ja042717i

APA

Abad, J. M., Mertens, S. F. L., Pita, M., Fernández, V. M., & Schiffrin, D. J. (2005). Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins. Journal of the American Chemical Society, 127(15), 5689-5694. https://doi.org/10.1021/ja042717i

Vancouver

Abad JM, Mertens SFL, Pita M, Fernández VM, Schiffrin DJ. Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins. Journal of the American Chemical Society. 2005;127(15):5689-5694. https://doi.org/10.1021/ja042717i

Author

Abad, J.M. ; Mertens, S.F.L. ; Pita, M. ; Fernández, V.M. ; Schiffrin, D.J. / Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins. In: Journal of the American Chemical Society. 2005 ; Vol. 127, No. 15. pp. 5689-5694.

Bibtex

@article{b90342f577ee4eca996b748d1a1b7704,
title = "Functionalization of thioctic acid-capped gold nanoparticles for specific immobilization of histidine-tagged proteins",
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. {\textcopyright} 2005 American Chemical Society.",
keywords = "Adsorption, Amino acids, Chemical modification, Copper, Enzyme immobilization, Gold, Proteins, Surface treatment, Functionalization, Gold clusters, Histadine-tagged proteins, Thioctic acid-capped gold nanoparticles, Nanostructured materials, cobalt, enzyme, ferredoxin nicotinamide adenine dinucleotide phosphate reductase, gold, histidine, horseradish peroxidase, nanoparticle, thioctic acid, transition element, adsorption, article, genetic engineering, protein binding, protein function, Binding Sites, Cobalt, Enzymes, Immobilized, Ferredoxin-NADP Reductase, Histidine, Horseradish Peroxidase, Ligands, Nanostructures, Spectrophotometry, Ultraviolet, Spectroscopy, Fourier Transform Infrared, Substrate Specificity, Thioctic Acid, Water",
author = "J.M. Abad and S.F.L. Mertens and M. Pita and V.M. Fern{\'a}ndez and D.J. Schiffrin",
year = "2005",
doi = "10.1021/ja042717i",
language = "English",
volume = "127",
pages = "5689--5694",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "AMER CHEMICAL SOC",
number = "15",

}

RIS

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 -