Carbon Nanotubes Arranged As Smart Interfaces in Lipid Langmuir-Blodgett Films Enhancing the Enzymatic Properties of Penicillinase for Biosensing Applications

Página do item simplificado
dc.citation.issue36
dc.citation.volume9
dc.contributor.authorScholl, Fabio A. [UNIFESP]
dc.contributor.authorMorais, Paulo V.
dc.contributor.authorGabriel, Rayla C.
dc.contributor.authorSchoening, Michael J.
dc.contributor.authorSiqueira, Jose R., Jr.
dc.contributor.authorCaseli, Luciano [UNIFESP]
dc.coverageWashington
dc.date.accessioned2020-08-04T13:40:11Z
dc.date.available2020-08-04T13:40:11Z
dc.date.issued2017
dc.description.abstractIn this paper, carbon nanotubes (CNTs) were incorporated in penicillinase-phospholipid Langmuir and Langmuir-Blodgett (LB) films to enhance the enzyme catalytic properties. Adsorption of the penicillinase and CNTs at dimyristoylphosphatidic acid (DMPA) monolayers at the air-water interface was investigated by surface pressure-area isotherms, vibrational spectroscopy, and Brewster angle microscopy. The floating monolayers were transferred to solid supports through the LB technique, forming mixed DMPA-CNTs-PEN films, which were investigated by I quartz crystal microbalance, vibrational spectroscopy, and atomic force microscopy. Enzyme activity was studied with UV-vis spectroscopy and the feasibility of the supramolecular device nanostructured as ultrathin films were essayed in a capacitive electrolyte-insulator-semiconductor (EIS) sensor device. The presence of CNTs in the enzyme-lipid LB film not only tuned the catalytic activity of penicillinase but also helped conserve its enzyme activity after weeks, showing increased values of activity. Viability as penicillin sensor was demonstrated with capacitance/voltage and constant capacitance measurements, exhibiting regular and distinctive output signals over all concentrations used in this work. These results may be related not only to the nanostructured system provided by the film, but also to the synergism between the compounds on the active layer, leading to a surface morphology that allowed a fast analyte diffusion because of an adequate molecular accommodation, which also preserved the penicillinase activity. This work therefore demonstrates the feasibility of employing LB films composed of lipids, CNTs, and enzymes as EIS devices for biosensing applications.en
dc.description.affiliationFed Univ Sao Paulo UNIFESP, Inst Environm Chem & Pharmaceut Sci, BR-09913030 Diadema, SP, Brazil
dc.description.affiliationFed Univ Triangulo Mineiro UFTM, Inst Exact Sci Nat & Educ, BR-38064200 Uberaba, MG, Brazil
dc.description.affiliationFH Aachen, INB, Campus Julich, D-52428 Julich, Germany
dc.description.affiliationForschungszentrum Julich, Peter Grunberg Inst PGI 8, D-52425 Julich, Germany
dc.description.affiliationUnifespFed Univ Sao Paulo UNIFESP, Inst Environm Chem & Pharmaceut Sci, BR-09913030 Diadema, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCNPq
dc.description.sponsorshipFAPESP
dc.description.sponsorshipFAPEMIG
dc.description.sponsorshipIDCNPq: 477668/2013-5
dc.description.sponsorshipIDFAPESP: 2015/10851-0
dc.description.sponsorshipIDFAPEMIG: APQ-00756-16
dc.description.sponsorshipIDFAPEMIG: CEX-RED-00010-14 RQ-MG
dc.format.extent31054-31066
dc.identifierhttp://dx.doi.org/10.1021/acsami.7b08095
dc.identifier.citationAcs Applied Materials & Interfaces. Washington, v. 9, n. 36, p. 31054-31066, 2017.
dc.identifier.doi10.1021/acsami.7b08095
dc.identifier.issn1944-8244
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/57358
dc.identifier.wosWOS:000411043600089
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofAcs Applied Materials & Interfaces
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectcarbon nanotubesen
dc.subjectLangmuir-Blodgett filmsen
dc.subjectcapacitive field-effect devicesen
dc.subjectbiosensorsen
dc.subjectsmart interfacesen
dc.titleCarbon Nanotubes Arranged As Smart Interfaces in Lipid Langmuir-Blodgett Films Enhancing the Enzymatic Properties of Penicillinase for Biosensing Applicationsen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
ICAQF - Artigos