Single-molecule detection with a millimetre-sized transistor
Eleonora Macchia,
Kyriaki Manoli,
Brigitte Holzer,
Cinzia Di Franco,
Matteo Ghittorelli,
Fabrizio Torricelli,
Domenico Alberga,
Giuseppe Felice Mangiatordi,
Gerardo Palazzo,
Gaetano Scamarcio and
Luisa Torsi ()
Additional contact information
Eleonora Macchia: Università degli Studi di Bari “Aldo Moro”
Kyriaki Manoli: Università degli Studi di Bari “Aldo Moro”
Brigitte Holzer: Università degli Studi di Bari “Aldo Moro”
Cinzia Di Franco: Istituto di Fotonica e Nanotecnologie
Matteo Ghittorelli: Università degli Studi di Brescia
Fabrizio Torricelli: Università degli Studi di Brescia
Domenico Alberga: Università degli Studi di Bari “Aldo Moro”
Giuseppe Felice Mangiatordi: Università degli Studi di Bari “Aldo Moro”
Gerardo Palazzo: Università degli Studi di Bari “Aldo Moro”
Gaetano Scamarcio: Istituto di Fotonica e Nanotecnologie
Luisa Torsi: Università degli Studi di Bari “Aldo Moro”
Nature Communications, 2018, vol. 9, issue 1, 1-10
Abstract:
Abstract Label-free single-molecule detection has been achieved so far by funnelling a large number of ligands into a sequence of single-binding events with few recognition elements host on nanometric transducers. Such approaches are inherently unable to sense a cue in a bulk milieu. Conceptualizing cells’ ability to sense at the physical limit by means of highly-packed recognition elements, a millimetric sized field-effect-transistor is used to detect a single molecule. To this end, the gate is bio-functionalized with a self-assembled-monolayer of 1012 capturing anti-Immunoglobulin-G and is endowed with a hydrogen-bonding network enabling cooperative interactions. The selective and label-free single molecule IgG detection is strikingly demonstrated in diluted saliva while 15 IgGs are assayed in whole serum. The suggested sensing mechanism, triggered by the affinity binding event, involves a work-function change that is assumed to propagate in the gating-field through the electrostatic hydrogen-bonding network. The proposed immunoassay platform is general and can revolutionize the current approach to protein detection.
Date: 2018
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-018-05235-z Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05235-z
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-018-05235-z
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().