Capacitance-modulated transistor detects odorant binding protein chiral interactions

Mohammad Yusuf Mulla, Elena Tuccori, Maria Magliulo, Gianluca Lattanzi, Gerardo Palazzo, Krishna Persaud and Luisa Torsi ()
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Mohammad Yusuf Mulla: Università degli Studi di Bari ‘Aldo Moro’
Elena Tuccori: School of Chemical Engineering and Analytical Science, The University of Manchester
Maria Magliulo: Università degli Studi di Bari ‘Aldo Moro’
Gianluca Lattanzi: INFN and TIRES, Università degli Studi di Bari ‘Aldo Moro’
Gerardo Palazzo: Università degli Studi di Bari ‘Aldo Moro’
Krishna Persaud: School of Chemical Engineering and Analytical Science, The University of Manchester
Luisa Torsi: Università degli Studi di Bari ‘Aldo Moro’

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract Peripheral events in olfaction involve odorant binding proteins (OBPs) whose role in the recognition of different volatile chemicals is yet unclear. Here we report on the sensitive and quantitative measurement of the weak interactions associated with neutral enantiomers differentially binding to OBPs immobilized through a self-assembled monolayer to the gate of an organic bio-electronic transistor. The transduction is remarkably sensitive as the transistor output current is governed by the small capacitance of the protein layer undergoing minute changes as the ligand–protein complex is formed. Accurate determination of the free-energy balances and of the capacitance changes associated with the binding process allows derivation of the free-energy components as well as of the occurrence of conformational events associated with OBP ligand binding. Capacitance-modulated transistors open a new pathway for the study of ultra-weak molecular interactions in surface-bound protein–ligand complexes through an approach that combines bio-chemical and electronic thermodynamic parameters.

Date: 2015
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DOI: 10.1038/ncomms7010

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