http://www.cnr.it/ontology/cnr/individuo/prodotto/ID10848
Highly conductive Redox protein-Carbon Nanotube Complex for Biosensing Applications (Articolo in rivista)
- Type
- Label
- Highly conductive Redox protein-Carbon Nanotube Complex for Biosensing Applications (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/adfm.201001650 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- C. Baldacchini; M. A. Herrero Chamorro; M. Prato; S. Cannistraro (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Biophysics and Nanoscience Centre and CNISM, Facoltà di Scienze, Università della Tuscia, Largo dell'Università
01100 Viterbo, Italy
Institute of Agro-environmental and Forest Biology - IBAF, National Research Council - CNR, Via Marconi 2, 05010 Porano, TR, Italy
Dipartimento di Scienze Farmaceutiche, Università di Trieste, Piazzale Europa 1, 34127 Trieste, Italy (literal)
- Titolo
- Highly conductive Redox protein-Carbon Nanotube Complex for Biosensing Applications (literal)
- Abstract
- The integration of redox proteins with nanomaterials has attracted much
interest in the past years, and metallic single-walled carbon nanotubes
(SWNTs) have been introduced as effi cient electrical wires to connect biomolecules
to metal electrodes in advanced nano-biodevices. Besides preserving
biofunctionality, the protein-nanotube connection should ensure appropriate
molecular orientation, fl exibility, and effi cient, reproducible electrical conduction.
In this respect, yeast cytochrome c redox proteins are connected to gold
electrodes through lying-down functionalized metallic SWNTs. Immobilization
of cytochromes to nanotubes is obtained via covalent bonding between the
exposed protein thiols and maleimide-terminated functional chains attached
to the carbon nanotubes. A single-molecule study performed by combining
scanning probe nanoscopies ascertains that the protein topological properties
are preserved upon binding and provides unprecedented current images
of single proteins bound to carbon nanotubes that allow a detailed I - V
characterization. Collectively, the results point out that the use as linkers of
suitably functionalized metallic SWNTs results in an electrical communication
between redox proteins and gold electrodes more effi cient and reproducible
than for proteins directly connected with metal surfaces. (literal)
- Prodotto di
- Autore CNR
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