Homogeneous protein analysis by magnetic core-shell nanorod probes

Handle URI:
http://hdl.handle.net/10754/604368
Title:
Homogeneous protein analysis by magnetic core-shell nanorod probes
Authors:
Schrittwieser, Stefan; Pelaz, Beatriz; Parak, Wolfgang J; Lentijo-Mozo, Sergio; Soulantica, Katerina; Dieckhoff, Jan; Ludwig, Frank; Altantzis, Thomas; Bals, Sara; Schotter, Joerg
Abstract:
Studying protein interactions is of vital importance both to fundamental biology research and to medical applications. Here, we report on the experimental proof of a universally applicable label-free homogeneous platform for rapid protein analysis. It is based on optically detecting changes in the rotational dynamics of magnetically agitated core-shell nanorods upon their specific interaction with proteins. By adjusting the excitation frequency, we are able to optimize the measurement signal for each analyte protein size. In addition, due to the locking of the optical signal to the magnetic excitation frequency, background signals are suppressed, thus allowing exclusive studies of processes at the nanoprobe surface only. We study target proteins (soluble domain of the human epidermal growth factor receptor 2 - sHER2) specifically binding to antibodies (trastuzumab) immobilized on the surface of our nanoprobes and demonstrate direct deduction of their respective sizes. Additionally, we examine the dependence of our measurement signal on the concentration of the analyte protein, and deduce a minimally detectable sHER2 concentration of 440 pM. For our homogeneous measurement platform, good dispersion stability of the applied nanoprobes under physiological conditions is of vital importance. To that end, we support our measurement data by theoretical modeling of the total particle-particle interaction energies. The successful implementation of our platform offers scope for applications in biomarker-based diagnostics as well as for answering basic biology questions.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Homogeneous protein analysis by magnetic core-shell nanorod probes 2016 ACS Applied Materials & Interfaces
Publisher:
American Chemical Society (ACS)
Journal:
ACS Applied Materials & Interfaces
Issue Date:
29-Mar-2016
DOI:
10.1021/acsami.5b11925
Type:
Article
ISSN:
1944-8244; 1944-8252
Sponsors:
The authors thank Frauke Alves, Julia Bode and Fernanda Ramos Gomes from the Max-Planck- Institute of Experimental Medicine in Göttingen for providing the trastuzumab antibody in form of the Herceptin therapeutic drug. The figure showing the measurement principle has been created by Darragh Crotty (www.darraghcrotty.com). Parts of this research were supported by the European Commission FP7 NAMDIATREAM project (EU NMP4-LA-2010–246479), by the German research foundation (DFG grant GRK 1782 to W.J.P.), and by the European Research Council (ERC Starting Grant #335078 Colouratom). B.P. acknowledges a PostDoctoral fellowship from the Alexander von Humboldt foundation.
Additional Links:
http://pubs.acs.org/doi/abs/10.1021/acsami.5b11925
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorSchrittwieser, Stefanen
dc.contributor.authorPelaz, Beatrizen
dc.contributor.authorParak, Wolfgang Jen
dc.contributor.authorLentijo-Mozo, Sergioen
dc.contributor.authorSoulantica, Katerinaen
dc.contributor.authorDieckhoff, Janen
dc.contributor.authorLudwig, Franken
dc.contributor.authorAltantzis, Thomasen
dc.contributor.authorBals, Saraen
dc.contributor.authorSchotter, Joergen
dc.date.accessioned2016-04-04T13:22:27Zen
dc.date.available2016-04-04T13:22:27Zen
dc.date.issued2016-03-29en
dc.identifier.citationHomogeneous protein analysis by magnetic core-shell nanorod probes 2016 ACS Applied Materials & Interfacesen
dc.identifier.issn1944-8244en
dc.identifier.issn1944-8252en
dc.identifier.doi10.1021/acsami.5b11925en
dc.identifier.urihttp://hdl.handle.net/10754/604368en
dc.description.abstractStudying protein interactions is of vital importance both to fundamental biology research and to medical applications. Here, we report on the experimental proof of a universally applicable label-free homogeneous platform for rapid protein analysis. It is based on optically detecting changes in the rotational dynamics of magnetically agitated core-shell nanorods upon their specific interaction with proteins. By adjusting the excitation frequency, we are able to optimize the measurement signal for each analyte protein size. In addition, due to the locking of the optical signal to the magnetic excitation frequency, background signals are suppressed, thus allowing exclusive studies of processes at the nanoprobe surface only. We study target proteins (soluble domain of the human epidermal growth factor receptor 2 - sHER2) specifically binding to antibodies (trastuzumab) immobilized on the surface of our nanoprobes and demonstrate direct deduction of their respective sizes. Additionally, we examine the dependence of our measurement signal on the concentration of the analyte protein, and deduce a minimally detectable sHER2 concentration of 440 pM. For our homogeneous measurement platform, good dispersion stability of the applied nanoprobes under physiological conditions is of vital importance. To that end, we support our measurement data by theoretical modeling of the total particle-particle interaction energies. The successful implementation of our platform offers scope for applications in biomarker-based diagnostics as well as for answering basic biology questions.en
dc.description.sponsorshipThe authors thank Frauke Alves, Julia Bode and Fernanda Ramos Gomes from the Max-Planck- Institute of Experimental Medicine in Göttingen for providing the trastuzumab antibody in form of the Herceptin therapeutic drug. The figure showing the measurement principle has been created by Darragh Crotty (www.darraghcrotty.com). Parts of this research were supported by the European Commission FP7 NAMDIATREAM project (EU NMP4-LA-2010–246479), by the German research foundation (DFG grant GRK 1782 to W.J.P.), and by the European Research Council (ERC Starting Grant #335078 Colouratom). B.P. acknowledges a PostDoctoral fellowship from the Alexander von Humboldt foundation.en
dc.language.isoenen
dc.publisherAmerican Chemical Society (ACS)en
dc.relation.urlhttp://pubs.acs.org/doi/abs/10.1021/acsami.5b11925en
dc.rightsThis document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Applied Materials & Interfaces, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/acsami.5b11925.en
dc.titleHomogeneous protein analysis by magnetic core-shell nanorod probesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalACS Applied Materials & Interfacesen
dc.eprint.versionPost-printen
dc.contributor.institutionMolecular Diagnostics, AIT Austrian Institute of Technology, Vienna, Austriaen
dc.contributor.institutionFachbereich Physik, Philipps-Universität Marburg, Marburg, Germanyen
dc.contributor.institutionCIC Biomagune, San Sebastian, Spainen
dc.contributor.institutionLaboratoire de Physique et Chimie des Nano-objets (LPCNO), Université de Toulouse; INSA, UPS, CNRS, Toulouse, Franceen
dc.contributor.institutionInstitute of Electrical Measurement and Fundamental Electrical Engineering, TU Braunschweig, Braunschweig, Germanyen
dc.contributor.institutionElectron Microscopy for Materials Research (EMAT), University of Antwerp, Antwerp, Belgiumen
dc.contributor.institutionDiagnostic and Interventional Radiology Department and Clinic, Universitätsklinikum Hamburg- Eppendorf (UKE), Hamburg, Germanyen
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)en
kaust.authorLentijo-Mozo, Sergioen
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