Journal article
Native desorption electrospray ionization liberates soluble and membrane protein complexes from surfaces
- Abstract:
- Mass spectrometry (MS) applications for intact protein complexes typically require electrospray (ES) ionization and have not been achieved via direct desorption from surfaces. Desorption ES ionization (DESI) MS has however transformed the study of tissue surfaces through release and characterisation of small molecules. Motivated by the desire to screen for ligand binding to intact protein complexes we report the development of a native DESI platform. By establishing conditions that preserve non‐covalent interactions we exploit the surface to capture a rapid turnover enzyme–substrate complex and to optimise detergents for membrane protein study. We demonstrate binding of lipids and drugs to membrane proteins deposited on surfaces and selectivity from a mix of related agonists for specific binding to a GPCR. Overall therefore we introduce this native DESI platform with the potential for high‐throughput ligand screening of some of the most challenging drug targets including GPCRs.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 4.3MB, Terms of use)
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- Publisher copy:
- 10.1002/anie.201704849
Authors
+ Wellcome Trust
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- Funding agency for:
- Robinson, C
- Grant:
- Investigator Award (104633/Z/14/Z)
+ Medical Research Council
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- Funding agency for:
- Robinson, C
- Grant:
- Investigator Award (104633/Z/14/Z)
+ European Research Council
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- Funding agency for:
- Robinson, C
- Grant:
- Investigator Award (104633/Z/14/Z)
- Publisher:
- Wiley
- Journal:
- Angewandte Chemie International Edition More from this journal
- Volume:
- 56
- Issue:
- 46
- Pages:
- 14463–14468
- Publication date:
- 2017-09-18
- Acceptance date:
- 2017-09-06
- DOI:
- EISSN:
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1521-3773
- ISSN:
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1433-7851
- Pmid:
-
28884954
- Language:
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English
- Keywords:
- Pubs id:
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pubs:730106
- UUID:
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uuid:52bb3fae-7c47-484a-85bc-500e72be2ee5
- Local pid:
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pubs:730106
- Source identifiers:
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730106
- Deposit date:
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2017-09-22
Terms of use
- Copyright holder:
- Ambrose et al
- Copyright date:
- 2017
- Notes:
-
Copyright © 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
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