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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Multifunctional biosensors based on peptide-polyelectrolyte conjugates

Full text
Author(s):
Kogikoski, Jr., S. [1] ; Sousa, C. P. [1] ; Liberato, M. S. [1] ; Andrade-Filho, T. [2] ; Prieto, T. [1] ; Ferreira, F. F. [1] ; Rocha, A. R. [3] ; Guha, S. [4] ; Alves, W. A. [1]
Total Authors: 9
Affiliation:
[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210580 Santo Andre, SP - Brazil
[2] Univ Fed Sul & Sudeste Para, Fac Fis, Inst Ciencias Exatas, Campus Maraba, BR-68505080 Maraba, Para - Brazil
[3] Univ Estadual Paulista UNESP, Inst Fis Teor, Sao Paulo, SP - Brazil
[4] Univ Missouri, Dept Phys & Astron, Columbia, MO 65211 - USA
Total Affiliations: 4
Document type: Journal article
Source: Physical Chemistry Chemical Physics; v. 18, n. 4, p. 3223-3233, JAN 28 2016.
Web of Science Citations: 11
Abstract

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 (P6(1)) and orthorhombic (P22(1)2(1)). 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. (AU)

FAPESP's process: 11/02346-6 - Modification of peptide nanostructures with potential application in biofuel cell
Grantee:Camila Pinheiro Sousa
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 12/15481-1 - Functional polymer matrices prepared by electrospinning: Studies of structural properties and biodegradation processes
Grantee:Michelle da Silva Liberato
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 13/12997-0 - Hierarchical self-organization of peptide amphiphiles: fundamental mechanisms and potential applications
Grantee:Wendel Andrade Alves
Support Opportunities: Regular Research Grants
FAPESP's process: 12/01933-8 - Biomimetic electrospun matrixes: possible application in NO detection
Grantee:Sergio Kogikoski Junior
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 08/57805-2 - Institute of Bioanalytics
Grantee:Lauro Tatsuo Kubota
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 11/11973-4 - ICTP South American Institute for Fundamental Research: a regional center for theoretical physics
Grantee:Nathan Jacob Berkovits
Support Opportunities: Research Projects - Thematic Grants