Fully automated characterization of protein-peptide binding by microfluidic 2D NMR
Fully automated characterization of protein-peptide binding by microfluidic 2D NMR
We demonstrate an automated microfluidic nuclear magnetic resonance (NMR) system that quantitatively characterizes protein-ligand interactions without user intervention and with minimal sample needs through protein-detected heteronuclear 2D NMR spectroscopy. Quantitation of protein-ligand interactions is of fundamental importance to the understanding of signaling and other life processes. As is well-known, NMR provides rich information both on the thermodynamics of binding and on the binding site. However, the required titrations are laborious and tend to require large amounts of sample, which are not always available. The present work shows how the analytical power of NMR detection can be brought in line with the trend of miniaturization and automation in life science workflows.
3204–3210
Plata, Marek
fa0e0a2a-0f55-4a6d-af90-761e5edbb2c1
Sharma, Manvendra
e249236d-221d-4e59-8440-011f6863f891
Utz, Marcel
c84ed64c-9e89-4051-af39-d401e423891b
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Plata, Marek
fa0e0a2a-0f55-4a6d-af90-761e5edbb2c1
Sharma, Manvendra
e249236d-221d-4e59-8440-011f6863f891
Utz, Marcel
c84ed64c-9e89-4051-af39-d401e423891b
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Plata, Marek, Sharma, Manvendra, Utz, Marcel and Werner, Jörn M.
(2022)
Fully automated characterization of protein-peptide binding by microfluidic 2D NMR.
Journal of the American Chemical Society, 145 (5), .
(doi:10.1021/jacs.2c13052).
Abstract
We demonstrate an automated microfluidic nuclear magnetic resonance (NMR) system that quantitatively characterizes protein-ligand interactions without user intervention and with minimal sample needs through protein-detected heteronuclear 2D NMR spectroscopy. Quantitation of protein-ligand interactions is of fundamental importance to the understanding of signaling and other life processes. As is well-known, NMR provides rich information both on the thermodynamics of binding and on the binding site. However, the required titrations are laborious and tend to require large amounts of sample, which are not always available. The present work shows how the analytical power of NMR detection can be brought in line with the trend of miniaturization and automation in life science workflows.
Text
jacs.2c13052
- Version of Record
More information
Accepted/In Press date: 30 January 2022
e-pub ahead of print date: 30 January 2022
Additional Information:
Funding Information:
This work has been supported by the European Commission Horizon 2020 programme (Future and Emerging Technologies OPEN Project TISuMR, grant number 737043). M.P. gratefully acknowledges a studentship from the Institute of Life Sciences, University of Southampton.
Publisher Copyright:
© 2023 The Authors. Published by American Chemical Society.
Identifiers
Local EPrints ID: 475376
URI: http://eprints.soton.ac.uk/id/eprint/475376
ISSN: 0002-7863
PURE UUID: 0a65170e-5587-46a1-92fe-8d8b1d6bed9e
Catalogue record
Date deposited: 16 Mar 2023 17:59
Last modified: 06 Jun 2024 01:51
Export record
Altmetrics
Contributors
Author:
Marek Plata
Author:
Manvendra Sharma
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics