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dc.contributor.author
Pfreundschuh, Moritz
dc.contributor.author
Alsteens, David
dc.contributor.author
Wieneke, Ralph
dc.contributor.author
Cheng, Zhang
dc.contributor.author
Coughlin, Shaun R.
dc.contributor.author
Tampé, Robert
dc.contributor.author
Kobilka, Brian K.
dc.contributor.author
Müller, Daniel J.
dc.date.accessioned
2018-09-07T10:55:55Z
dc.date.available
2017-06-11T20:55:17Z
dc.date.available
2018-09-07T10:55:55Z
dc.date.issued
2015-11
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/ncomms9857
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/106653
dc.identifier.doi
10.3929/ethz-b-000106653
dc.description.abstract
A current challenge in life sciences is to image cell membrane receptors while characterizing their specific interactions with various ligands. Addressing this issue has been hampered by the lack of suitable nanoscopic methods. Here we address this challenge and introduce multifunctional high-resolution atomic force microscopy (AFM) to image human protease-activated receptors (PAR1) in the functionally important lipid membrane and to simultaneously localize and quantify their binding to two different ligands. Therefore, we introduce the surface chemistry to bifunctionalize AFM tips with the native receptor-activating peptide and a tris-N-nitrilotriacetic acid (tris-NTA) group binding to a His10-tag engineered to PAR1. We further introduce ways to discern between the binding of both ligands to different receptor sites while imaging native PAR1s. Surface chemistry and nanoscopic method are applicable to a range of biological systems in vitro and in vivo and to concurrently detect and localize multiple ligand-binding sites at single receptor resolution.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Identifying and quantifying two ligand-binding sites while imaging native human membrane receptors by AFM
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2015-11-12
ethz.journal.title
Nature Communications
ethz.journal.volume
6
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
8857
en_US
ethz.size
7 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
Multifunktionelles hochauflösendes Abbilden und Kartieren der Kraftfelder biologischer Membranen und Membranproteine
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.nebis
007044158
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02060 - Dep. Biosysteme / Dep. of Biosystems Science and Eng.::03870 - Müller, Daniel J. / Müller, Daniel J.
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02060 - Dep. Biosysteme / Dep. of Biosystems Science and Eng.::03870 - Müller, Daniel J. / Müller, Daniel J.
ethz.grant.agreementno
134521
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projektförderung in Mathematik, Natur- und Ingenieurwissenschaften (Abteilung II)
ethz.date.deposited
2017-06-11T20:56:08Z
ethz.source
ECIT
ethz.identifier.importid
imp593653ab3e0c046924
ethz.ecitpid
pub:166915
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-15T06:05:16Z
ethz.rosetta.lastUpdated
2019-02-03T05:27:10Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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