Abstract
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 |
|---|---|
| Article number | 8687 |
| Number of pages | 8 |
| Journal | Scientific Reports |
| Volume | 5 |
| DOIs | |
| Publication status | Published - 3 Mar 2015 |
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Protein phosphorylation detection using dual-mode field-effect devices and nanoplasmonic sensors. / Bhalla, Nikhil; Di Lorenzo, Mirella; Pula, Giordano; Estrela, Pedro.
In: Scientific Reports, Vol. 5, 8687, 03.03.2015.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Protein phosphorylation detection using dual-mode field-effect devices and nanoplasmonic sensors
AU - Bhalla, Nikhil
AU - Di Lorenzo, Mirella
AU - Pula, Giordano
AU - Estrela, Pedro
PY - 2015/3/3
Y1 - 2015/3/3
N2 - 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.
AB - 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.
UR - http://dx.doi.org/10.1038/srep08687
U2 - 10.1038/srep08687
DO - 10.1038/srep08687
M3 - Article
VL - 5
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
M1 - 8687
ER -