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Specific and oriented immobilization of proteins on gold nanoparticles

Research output: Contribution to conference - Without ISBN/ISSN Posterpeer-review

Published

Standard

Specific and oriented immobilization of proteins on gold nanoparticles. / Vaz Dominguez, Cristina; Abad, José M. ; Mertens, Stijn et al.
2005. Poster session presented at Trends in Nanotechnology, Oviedo, Spain.

Research output: Contribution to conference - Without ISBN/ISSN Posterpeer-review

Harvard

Vaz Dominguez, C, Abad, JM, Mertens, S, Pita, M, Fernánde, VM & Schiffrin, DJ 2005, 'Specific and oriented immobilization of proteins on gold nanoparticles', Trends in Nanotechnology, Oviedo, Spain, 29/08/05 - 2/09/05. <http://www.tntconf.org/2005/Abstracts/TNT05_Vaz.pdf>

APA

Vaz Dominguez, C., Abad, J. M., Mertens, S., Pita, M., Fernánde, V. M., & Schiffrin, D. J. (2005). Specific and oriented immobilization of proteins on gold nanoparticles. Poster session presented at Trends in Nanotechnology, Oviedo, Spain. http://www.tntconf.org/2005/Abstracts/TNT05_Vaz.pdf

Vancouver

Vaz Dominguez C, Abad JM, Mertens S, Pita M, Fernánde VM, Schiffrin DJ. Specific and oriented immobilization of proteins on gold nanoparticles. 2005. Poster session presented at Trends in Nanotechnology, Oviedo, Spain.

Author

Vaz Dominguez, Cristina ; Abad, José M. ; Mertens, Stijn et al. / Specific and oriented immobilization of proteins on gold nanoparticles. Poster session presented at Trends in Nanotechnology, Oviedo, Spain.2 p.

Bibtex

@conference{5b7a4702d94f4568ac8f7d8786bc205c,
title = "Specific and oriented immobilization of proteins on gold nanoparticles",
abstract = "Over the past years, there has been a noticeable interest on the coverage of goldsurfaces with monolayers of proteins based on the molecular recognition properties of biological systems T. In this sense, the immobilization of proteins on surfaces retaining their full activity and stability constitutes a challenging goal. Most of the common methods are difficult to control and usually yield randomly bound proteins. On the contrary, an ideal immobilization would produce saturation coverage of specifically bound proteins. The formation of protein layers is induced by anchoring them to gold surfaces functionalized with active molecules, such as transition metal complexes with affinity to repetitive histidine sequences. A feasible method to uniformly cover gold surfaces consists on the self-assembly of thiols by oxidative-chemisorption over the gold. Reversible monolayers of histidine-tagged proteins have been produced using agold layer covered with a chelator thioalkane monolayer. In order to avoid a highly complex organic synthetic work, step-by-step construction of the functional monolayer over a template of thiocarboxylic acid chemisorbed onto gold has been developed.Because of its simplicity, both, from a conceptual as well as from a practicalpoint of view, the step-by-step synthesis of a functional self assembled monolayer is accessible to most of the laboratories working on enzyme technology in spite of having limited facilities for organic synthesis. This synthetic strategy allows, by a judicious design of the synthetic route, the development of a multiplicity of architectures on SAMs. Different SAM strategies have been developed in our group for controlled and oriented immobilization of enzymes onto gold surfaces, using them as amperometric electrodes in the characterization of the enzymatic catalytic performance.We present a next step of these SAM strategies towards functionalization of goldnanoparticles{\textquoteright} surface for oriented immobilization of model proteins. The SAMprovides the ability to discriminate between specific and non-specific proteinsattachment. ",
author = "{Vaz Dominguez}, Cristina and Abad, {Jos{\'e} M.} and Stijn Mertens and Marcos Pita and Fern{\'a}nde, {Victor M.} and Schiffrin, {David J.}",
year = "2005",
language = "English",
note = "Trends in Nanotechnology ; Conference date: 29-08-2005 Through 02-09-2005",

}

RIS

TY - CONF

T1 - Specific and oriented immobilization of proteins on gold nanoparticles

AU - Vaz Dominguez, Cristina

AU - Abad, José M.

AU - Mertens, Stijn

AU - Pita, Marcos

AU - Fernánde, Victor M.

AU - Schiffrin, David J.

PY - 2005

Y1 - 2005

N2 - Over the past years, there has been a noticeable interest on the coverage of goldsurfaces with monolayers of proteins based on the molecular recognition properties of biological systems T. In this sense, the immobilization of proteins on surfaces retaining their full activity and stability constitutes a challenging goal. Most of the common methods are difficult to control and usually yield randomly bound proteins. On the contrary, an ideal immobilization would produce saturation coverage of specifically bound proteins. The formation of protein layers is induced by anchoring them to gold surfaces functionalized with active molecules, such as transition metal complexes with affinity to repetitive histidine sequences. A feasible method to uniformly cover gold surfaces consists on the self-assembly of thiols by oxidative-chemisorption over the gold. Reversible monolayers of histidine-tagged proteins have been produced using agold layer covered with a chelator thioalkane monolayer. In order to avoid a highly complex organic synthetic work, step-by-step construction of the functional monolayer over a template of thiocarboxylic acid chemisorbed onto gold has been developed.Because of its simplicity, both, from a conceptual as well as from a practicalpoint of view, the step-by-step synthesis of a functional self assembled monolayer is accessible to most of the laboratories working on enzyme technology in spite of having limited facilities for organic synthesis. This synthetic strategy allows, by a judicious design of the synthetic route, the development of a multiplicity of architectures on SAMs. Different SAM strategies have been developed in our group for controlled and oriented immobilization of enzymes onto gold surfaces, using them as amperometric electrodes in the characterization of the enzymatic catalytic performance.We present a next step of these SAM strategies towards functionalization of goldnanoparticles’ surface for oriented immobilization of model proteins. The SAMprovides the ability to discriminate between specific and non-specific proteinsattachment.

AB - Over the past years, there has been a noticeable interest on the coverage of goldsurfaces with monolayers of proteins based on the molecular recognition properties of biological systems T. In this sense, the immobilization of proteins on surfaces retaining their full activity and stability constitutes a challenging goal. Most of the common methods are difficult to control and usually yield randomly bound proteins. On the contrary, an ideal immobilization would produce saturation coverage of specifically bound proteins. The formation of protein layers is induced by anchoring them to gold surfaces functionalized with active molecules, such as transition metal complexes with affinity to repetitive histidine sequences. A feasible method to uniformly cover gold surfaces consists on the self-assembly of thiols by oxidative-chemisorption over the gold. Reversible monolayers of histidine-tagged proteins have been produced using agold layer covered with a chelator thioalkane monolayer. In order to avoid a highly complex organic synthetic work, step-by-step construction of the functional monolayer over a template of thiocarboxylic acid chemisorbed onto gold has been developed.Because of its simplicity, both, from a conceptual as well as from a practicalpoint of view, the step-by-step synthesis of a functional self assembled monolayer is accessible to most of the laboratories working on enzyme technology in spite of having limited facilities for organic synthesis. This synthetic strategy allows, by a judicious design of the synthetic route, the development of a multiplicity of architectures on SAMs. Different SAM strategies have been developed in our group for controlled and oriented immobilization of enzymes onto gold surfaces, using them as amperometric electrodes in the characterization of the enzymatic catalytic performance.We present a next step of these SAM strategies towards functionalization of goldnanoparticles’ surface for oriented immobilization of model proteins. The SAMprovides the ability to discriminate between specific and non-specific proteinsattachment.

M3 - Poster

T2 - Trends in Nanotechnology

Y2 - 29 August 2005 through 2 September 2005

ER -