Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/42764
DC FieldValueLanguage
dc.contributor.authorBaldacchini, Chiarait
dc.contributor.authorBizzarri, Anna Ritait
dc.contributor.authorCannistraro, Salvatoreit
dc.date.accessioned2021-02-09T08:16:43Z-
dc.date.available2021-02-09T08:16:43Z-
dc.date.issued2016it
dc.identifier.issn0014-3057it
dc.identifier.urihttp://hdl.handle.net/2067/42764-
dc.description.abstractThe efficient implementation of functional biomolecules into hybrid devices is a central topic in current material science research, and redox metalloproteins often emerged as promising candidates. In particular, the blue copper protein Azurin (AZ) is highly suitable for future integrations in bio-optoelectronic nanodevices and biosensors, since it is characterized by a very fast and efficient intramolecular electron transfer, and it shows a marked structural robustness once adsorbed on surfaces; this allowing the preservation of its physiological functions. In addition, AZ bears an exposed disulphide group, suitable for covalent anchoring on gold, allowing thus a controlled orientation of the protein and a good electrical coupling with the electrode. Moreover, AZ shows an interesting interplay among its redox, optical and vibrational properties, somewhat connected with its biorecognition capabilities towards several substrates. We present here an extensive overview of our results on the functional properties of AZ once adsorbed on surfaces, together with a critical comparison with recently published studies. We mainly focus on its electron transfer, conduction and biorecognition capability, also in connection with external visible light and voltage excitation. We, moreover, outline the development of suitable surface assembling strategies that could ensure both the preservation of the biomolecule physiological characteristics and the establishing of a reliable connection with the electrical/optical read out. A particular emphasis is given to the extensive application of the Scanning Probe Microscopies that could allow a detailed characterization of the hybrid systems at the single-biomolecule level, disclosing aspects otherwise hidden when bulk techniques are being used.it
dc.format.mediumSTAMPAit
dc.language.isoengit
dc.titleElectron transfer, conduction and biorecognition properties of the redox metalloprotein Azurin assembled onto inorganic substratesit
dc.typearticle*
dc.identifier.doi10.1016/j.eurpolymj.2016.04.030it
dc.identifier.scopus2-s2.0-84964869550it
dc.identifier.isi000385595300036it
dc.identifier.urlhttps://www.sciencedirect.com/science/article/pii/S0014305716303123?via%3Dihubit
dc.relation.journalEUROPEAN POLYMER JOURNALit
dc.relation.firstpage407it
dc.relation.lastpage427it
dc.relation.volume83it
dc.subject.keywordselectron transferit
dc.subject.keywordsazurinit
dc.subject.keywordscopper proteinsit
dc.description.numberofauthors3it
dc.description.internationalnoit
dc.contributor.countryITAit
dc.type.refereeREF_1it
dc.type.miur262*
item.fulltextWith Fulltext-
item.openairetypearticle-
item.cerifentitytypePublications-
item.grantfulltextrestricted-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.journal.journalissn0014-3057-
crisitem.journal.anceE060843-
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