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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Water-gated phthalocyanine transistors: Operation and transduction of the peptide-enzyme interaction

Texto completo
de Oliveira, Rafael Furlan [1] ; Merces, Leandro [1, 2] ; Vello, Tatiana Parra [1, 3] ; Bof Bufon, Carlos Cesar [1, 2, 3]
Número total de Autores: 4
Afiliação do(s) autor(es):
[1] CNPEM, Brazilian Nanotechnol Natl Lab LNNano, BR-13083970 Campinas, SP - Brazil
[2] Univ Estadual Campinas, Inst Phys Gleb Wataghin IFGW, BR-13083859 Campinas, SP - Brazil
[3] Univ Estadual Campinas, Inst Chem IQ, Dept Phys Chem, BR-13083970 Campinas, SP - Brazil
Número total de Afiliações: 3
Tipo de documento: Artigo Científico
Fonte: ORGANIC ELECTRONICS; v. 31, p. 217-226, APR 2016.
Citações Web of Science: 16

The use of aqueous solutions as the gate medium is an attractive strategy to obtain high charge carrier density (10(12) cm(-2)) and low operational voltages (<1 V) in organic transistors. Additionally, it provides a simple and favorable architecture to couple both ionic and electronic domains in a single device, which is crucial for the development of novel technologies in bioelectronics. Here, we demonstrate the operation of transistors containing copper phthalocyanine (CuPc) thin-films gated with water and discuss the charge dynamics at the CuPc/water interface. Without the need for complex multilayer patterning, or the use of surface treatments, water-gated CuPc transistors exhibited low threshold (100 +/- 20 mV) and working voltages (<1 V) compared to conventional CuPc transistors, along with similar charge carrier mobilities (1.2 +/- 0.2) x 10(-3) cm(2) V-1 s(-1). Several device characteristics such as moderate switching speeds and hysteresis, associated with high capacitances at low frequencies upon bias application (3.4 -12 mu F cm(-2)), indicate the occurrence of interfacial ion doping. Finally, water-gated CuPc OTFTs were employed in the transduction of the biospecific interaction between tripeptide reduced glutathione (GSH) and glutathione S-transferase (GST) enzyme, taking advantage of the device sensitivity and multiparametricity. (C) 2016 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 13/22127-2 - Desenvolvimento de novos materiais estratégicos para dispositivos analíticos integrados
Beneficiário:Lauro Tatsuo Kubota
Linha de fomento: Auxílio à Pesquisa - Temático