Multifunctional biosensors based on peptide–polyelectrolyte conjugates. Issue 4 (8th January 2016)
- Record Type:
- Journal Article
- Title:
- Multifunctional biosensors based on peptide–polyelectrolyte conjugates. Issue 4 (8th January 2016)
- Main Title:
- Multifunctional biosensors based on peptide–polyelectrolyte conjugates
- Authors:
- Kogikoski, S.
Sousa, C. P.
Liberato, M. S.
Andrade-Filho, T.
Prieto, T.
Ferreira, F. F.
Rocha, A. R.
Guha, S.
Alves, W. A. - Abstract:
- Abstract : The crystal structure of self-assembled peptide nanostructures dictates the conductivity. We show that the orthorhombic phase can be doped with PAH, improving hole and electron injection, opening opportunities for self-assembled peptide composites. Abstract : A novel enzymatic platform for the sensing of H2 O2 and glucose that usesl, 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 ( P 61 ) and orthorhombic ( P 221 21 ). 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 forAbstract : The crystal structure of self-assembled peptide nanostructures dictates the conductivity. We show that the orthorhombic phase can be doped with PAH, improving hole and electron injection, opening opportunities for self-assembled peptide composites. Abstract : A novel enzymatic platform for the sensing of H2 O2 and glucose that usesl, 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 ( P 61 ) and orthorhombic ( P 221 21 ). 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. … (more)
- Is Part Of:
- Physical chemistry chemical physics. Volume 18:Issue 4(2016)
- Journal:
- Physical chemistry chemical physics
- Issue:
- Volume 18:Issue 4(2016)
- Issue Display:
- Volume 18, Issue 4 (2016)
- Year:
- 2016
- Volume:
- 18
- Issue:
- 4
- Issue Sort Value:
- 2016-0018-0004-0000
- Page Start:
- 3223
- Page End:
- 3233
- Publication Date:
- 2016-01-08
- Subjects:
- Chemistry, Physical and theoretical -- Periodicals
541.3 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/cp#!issueid=cp016040&type=current&issnprint=1463-9076 ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c5cp07165h ↗
- Languages:
- English
- ISSNs:
- 1463-9076
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6475.306000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 5080.xml