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Long-Term Storage of Surface-Adsorbed Protein Machines

[Image: see text] The effective and simple long-term storage of complex functional proteins is critical in achieving commercially viable biosensors. This issue is particularly challenging in recently proposed types of nanobiosensors, where molecular-motor-driven transportation substitutes microfluid...

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Detalles Bibliográficos
Autores principales: Albet-Torres, Nuria, Månsson, Alf
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2011
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3104519/
https://www.ncbi.nlm.nih.gov/pubmed/21563803
http://dx.doi.org/10.1021/la201081w
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author Albet-Torres, Nuria
Månsson, Alf
author_facet Albet-Torres, Nuria
Månsson, Alf
author_sort Albet-Torres, Nuria
collection PubMed
description [Image: see text] The effective and simple long-term storage of complex functional proteins is critical in achieving commercially viable biosensors. This issue is particularly challenging in recently proposed types of nanobiosensors, where molecular-motor-driven transportation substitutes microfluidics and forms the basis for novel detection schemes. Importantly, therefore, we here describe that delicate heavy meromyosin (HMM)-based nanodevices (HMM motor fragments adsorbed to silanized surfaces and actin bound to HMM) fully maintain their function when stored at −20 °C for more than a month. The mechanisms for the excellent preservation of acto-HMM motor function upon repeated freeze–thaw cycles are discussed. The results are important to the future commercial implementation of motor-based nanodevices and are of more general value to the long-term storage of any protein-based bionanodevice.
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spelling pubmed-31045192011-05-31 Long-Term Storage of Surface-Adsorbed Protein Machines Albet-Torres, Nuria Månsson, Alf Langmuir [Image: see text] The effective and simple long-term storage of complex functional proteins is critical in achieving commercially viable biosensors. This issue is particularly challenging in recently proposed types of nanobiosensors, where molecular-motor-driven transportation substitutes microfluidics and forms the basis for novel detection schemes. Importantly, therefore, we here describe that delicate heavy meromyosin (HMM)-based nanodevices (HMM motor fragments adsorbed to silanized surfaces and actin bound to HMM) fully maintain their function when stored at −20 °C for more than a month. The mechanisms for the excellent preservation of acto-HMM motor function upon repeated freeze–thaw cycles are discussed. The results are important to the future commercial implementation of motor-based nanodevices and are of more general value to the long-term storage of any protein-based bionanodevice. American Chemical Society 2011-05-12 2011-06-07 /pmc/articles/PMC3104519/ /pubmed/21563803 http://dx.doi.org/10.1021/la201081w Text en Copyright © 2011 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Albet-Torres, Nuria
Månsson, Alf
Long-Term Storage of Surface-Adsorbed Protein Machines
title Long-Term Storage of Surface-Adsorbed Protein Machines
title_full Long-Term Storage of Surface-Adsorbed Protein Machines
title_fullStr Long-Term Storage of Surface-Adsorbed Protein Machines
title_full_unstemmed Long-Term Storage of Surface-Adsorbed Protein Machines
title_short Long-Term Storage of Surface-Adsorbed Protein Machines
title_sort long-term storage of surface-adsorbed protein machines
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3104519/
https://www.ncbi.nlm.nih.gov/pubmed/21563803
http://dx.doi.org/10.1021/la201081w
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