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Issue 4, 2016
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Multifunctional biosensors based on peptide–polyelectrolyte conjugates

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A novel enzymatic platform for the sensing of H2O2 and glucose that uses L,L-diphenylalanine micro/nanostructures (FF-MNSs) as an enzyme support is shown. This platform is obtained by the self-assembly of poly(allylamine hydrochloride) (PAH), FF-MNSs, and microperoxidase-11 (MP11) anchored onto the peptide matrix, in two different crystal structures of FF-MNSs: hexagonal (P61) and orthorhombic (P22121). The electroactive area of the electrodes increases in the presence of FF-MNSs. We also demonstrate via theoretical calculations that the valence band energy of the orthorhombic structure allows it to be doped, similarly to p-type semiconductors, where PAH acts as a doping agent for the orthorhombic peptide structure, decreasing the band-gap by around 1 eV, which results in a smaller charge transfer resistance. These results are consistent with electrochemical impedance spectroscopy measurements, which further elucidate the role of the band structure of the orthorhombic FF-MNSs in the conductivity and electron transfer rates of the hybrid material. An effective communication between the electrode and the active site of a glucose oxidase enzyme through MP11–protein complexes occurs, paving the way for FF-MNSs in the orthorhombic phase for the future development of bioelectronics sensing devices.

Graphical abstract: Multifunctional biosensors based on peptide–polyelectrolyte conjugates

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The article was received on 20 Nov 2015, accepted on 22 Dec 2015 and first published on 22 Dec 2015

Article type: Paper
DOI: 10.1039/C5CP07165H
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Citation: Phys. Chem. Chem. Phys., 2016,18, 3223-3233
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    Multifunctional biosensors based on peptide–polyelectrolyte conjugates

    S. Kogikoski, C. P. Sousa, M. S. Liberato, T. Andrade-Filho, T. Prieto, F. F. Ferreira, A. R. Rocha, S. Guha and W. A. Alves, Phys. Chem. Chem. Phys., 2016, 18, 3223
    DOI: 10.1039/C5CP07165H

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