Projects per year
Abstract
Phosphorylation by kinases is an important post-translational modification of proteins. It is a critical control for the regulation of vital cellular activities, and its dysregulation is implicated in several diseases. A common drug discovery approach involves, therefore, time-consuming screenings of large libraries of candidate compounds to identify novel inhibitors of protein kinases.
In this work, we propose a novel method that combines localized surface plasmon resonance (LSPR) and electrolyte insulator semiconductor (EIS)-based proton detection for the rapid identification of novel protein kinase inhibitors. In particular, the selective detection of thiophosphorylated proteins by LSPR is achieved by changing their resonance properties via a pre-binding with gold nanoparticles. In parallel, the EIS field-effect structure allows the real-time electrochemical monitoring of the protein phosphorylation by detecting the release of protons associated with the kinases activity. This innovative combination of both field-effect and nanoplasmonic sensing makes the detection of protein phosphorylation more reliable and effective. As a result, the screening of protein kinase inhibitors becomes more rapid, sensitive, robust and cost-effective.
In this work, we propose a novel method that combines localized surface plasmon resonance (LSPR) and electrolyte insulator semiconductor (EIS)-based proton detection for the rapid identification of novel protein kinase inhibitors. In particular, the selective detection of thiophosphorylated proteins by LSPR is achieved by changing their resonance properties via a pre-binding with gold nanoparticles. In parallel, the EIS field-effect structure allows the real-time electrochemical monitoring of the protein phosphorylation by detecting the release of protons associated with the kinases activity. This innovative combination of both field-effect and nanoplasmonic sensing makes the detection of protein phosphorylation more reliable and effective. As a result, the screening of protein kinase inhibitors becomes more rapid, sensitive, robust and cost-effective.
Original language | English |
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Article number | 8687 |
Number of pages | 8 |
Journal | Scientific Reports |
Volume | 5 |
DOIs | |
Publication status | Published - 3 Mar 2015 |
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Projects
- 1 Finished
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Paracrine Regulation of Endothelial Cell Motility
Pula, G.
Biotechnology and Biological Sciences Research Council
15/05/12 → 14/05/15
Project: Research council
Profiles
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Mirella Di Lorenzo
- Department of Chemical Engineering - Reader
- Centre for Sustainable and Circular Technologies (CSCT)
- EPSRC Centre for Doctoral Training in Statistical Applied Mathematics (SAMBa)
- Water Innovation and Research Centre (WIRC)
- Reaction and Catalysis Engineering research unit (RaCE)
- Centre for Biosensors, Bioelectronics and Biodevices (C3Bio)
- Centre for Integrated Bioprocessing Research (CIBR)
Person: Research & Teaching
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Pedro Estrela
- Department of Electronic & Electrical Engineering - Senior Lecturer
- Centre for Biosensors, Bioelectronics and Biodevices (C3Bio)
- Centre for Therapeutic Innovation
- Centre for Sustainable and Circular Technologies (CSCT)
- Water Innovation and Research Centre (WIRC)
- Centre for Nanoscience and Nanotechnology
Person: Research & Teaching
Equipment
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MC2- Surface analysis and spectroscopy
Material and Chemical Characterisation (MC2)Facility/equipment: Technology type