An SECM study on the influence of cationic, membrane-active peptides on a gold-supported self-assembled monolayer


Autoria(s): Abdelhamid, Muhammad E.; Piantavigna, Stefania; Bond, Alan M.; Graham, Bim; Spiccia, Leone; Martin, Lisandra L.; O'Mullane, Anthony P.
Data(s)

01/02/2015

Resumo

The influence of the membrane active peptides, Tat44–57 (activator in HIV-1) and melittin (active content of bee venom), on self-assembled monolayers of 6-mercaptohexanoic acid (MHA) on gold electrodes has been studied with scanning electrochemical microscopy (SECM). It was found that MHA, when deprotonated at physiological pH, significantly affected the relative rates of electron transfer between the [Fe(CN)6]4− solution based mediator and the underlying gold electrode, predominantly by the electrostatic interaction between the mediator and MHA. Upon the introduction of Tat44–57 ormelittin to the electrolyte, the relative rate of electron transfer through the MHA layer could be increased or decreased depending on the mediator used. However, in all cases it was found that these peptides have the ability to be incorporated into synthetic SAMs, which has implications for future electrochemical studies carried out using cell mimicking membranes immobilised on such layers.

Formato

application/pdf

Identificador

http://eprints.qut.edu.au/79521/

Publicador

Elsevier Inc.

Relação

http://eprints.qut.edu.au/79521/1/SECM_peptide.pdf

DOI:10.1016/j.elecom.2014.11.018

Abdelhamid, Muhammad E., Piantavigna, Stefania, Bond, Alan M., Graham, Bim, Spiccia, Leone, Martin, Lisandra L., & O'Mullane, Anthony P. (2015) An SECM study on the influence of cationic, membrane-active peptides on a gold-supported self-assembled monolayer. Electrochemistry Communications, 51, pp. 11-14.

Direitos

Copyright 2014 Elsevier B.V.

NOTICE: this is the author’s version of a work that was accepted for publication in Electrochemistry Communications. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Electrochemistry Communications, Volume 51, February 2015, DOI: 10.1016/j.elecom.2014.11.018

Fonte

School of Chemistry, Physics & Mechanical Engineering; Science & Engineering Faculty

Palavras-Chave #030604 Electrochemistry #Scanning electrochemical microscopy #Self-assembled monolayers #Peptides #Electron transfer #Electrochemistry
Tipo

Journal Article