• 14 Citations

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.
LanguageEnglish
Article number8687
Number of pages8
JournalScientific Reports
Volume5
DOIs
StatusPublished - 3 Mar 2015

Fingerprint

Phosphorylation
Protein Kinase Inhibitors
Sensors
Surface plasmon resonance
Electrolytes
Protons
Screening
Proteins
Phosphotransferases
Semiconductor materials
Gold
Nanoparticles
Monitoring
Costs

Cite this

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 journalArticle

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AU - Di Lorenzo,Mirella

AU - Pula,Giordano

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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.

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