Development of new well-defined multifunctional dendrimers for applications in nan...
| 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: | 14 |
| 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 type: | Scholarships in Brazil - Doctorate (Direct) |
| FAPESP's process: | 13/12997-0 - Hierarchical self-organization of peptide amphiphiles: fundamental mechanisms and potential applications |
| Grantee: | Wendel Andrade Alves |
| Support type: | Regular Research Grants |
| FAPESP's process: | 12/01933-8 - Biomimetic electrospun matrixes: possible application in NO detection |
| Grantee: | Sergio Kogikoski Junior |
| Support type: | Scholarships in Brazil - Doctorate (Direct) |
| FAPESP's process: | 11/11973-4 - ICTP South American Institute for Fundamental Research: a regional center for theoretical physics |
| Grantee: | Nathan Jacob Berkovits |
| Support type: | Research Projects - Thematic Grants |
| 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 type: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 08/57805-2 - Institute of Bioanalytics |
| Grantee: | Lauro Tatsuo Kubota |
| Support type: | Research Projects - Thematic Grants |