Moraes, Marli L. [UNESP]Lima, Lais R. [UNESP]Silva, Robson R. [UNESP]Cavicchioli, Mauricio [UNESP]Ribeiro, Sidney J.L. [UNESP]2014-05-272014-05-272013-03-19Langmuir, v. 29, n. 11, p. 3829-3834, 2013.0743-74631520-5827http://hdl.handle.net/11449/74850The peptide NS5A-1 (PPLLESWKDPDYVPPWHG), derived from hepatitis C virus (HCV) NS5A protein, was immobilized into layer-by-layer (LbL) silk fibroin (SF) films. Deposition was monitored by UV-vis absorption measurements at each bilayer deposited. The interaction SF/peptide film induced secondary structure in NS5A-1 as indicated by fluorescence and circular dichroism (CD) measurements. Voltammetric sensor (SF/NS5A-1) properties were observed when the composite film was tested in the presence of anti-HCV. The peptide-silk fibroin interaction studied here showed new architectures for immunosensors based on antigenic peptides and SF as a suitable immobilization matrix. © 2013 American Chemical Society.3829-3834engAntigenic peptidesHepatitis C virusImmobilization matricesLayer-by-layersNanostructured FilmsSecondary structuresUV-vis absorptionsVoltammetric sensorAntigensComposite filmsImmunosensorsVirusesPeptidesantigenfibroinimmobilized proteinnanomaterialNS 5 protein, hepatitis C virusNS-5 protein, hepatitis C viruspeptide fragmentvirus proteinamino acid sequenceanimalchemistrygenetic proceduresimmunologymethodologymolecular geneticsAmino Acid SequenceAnimalsBiosensing TechniquesFibroinsImmobilized ProteinsMolecular Sequence DataNanostructuresPeptide FragmentsViral Nonstructural ProteinsArtigo10.1021/la304404vWOS:000316168400037Acesso restrito2-s2.0-84875304965