Charge transport in fibrous/not fibrous -helical and variant peptides

• Autor(a) principal: Bezerril, Leonardo Mafra
• Data de Publicação: 2011
• Outros Autores: Fulco, Umberto Laino, Oliveira, Jonas Ivan Nobre, Corso, Gilberto, Albuquerque, Eudenilson Lins de, Freire, V. N., Caetano, W. S.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFRN
• Texto Completo: https://repositorio.ufrn.br/handle/123456789/30964
• topic: Charge transport; Fibrous/not fibrous; Helical; Variant peptides

Although differing only by the Ala→Gln substitution at the fifth or seventh position of the 3-peptide amino acid sequence Leu-Glu-Thr-Leu-Ala-Lys-Ala3, the 5Q3 variant forms fibrous assemblies more attenuated than those of the 3-peptide, while the 7Q3 variant does not form fibrils. A tight-binding transport modeling was performed to obtain their current-voltage patterns, with hopping energies of the dipeptides calculated within the density functional theory framework. Beyond the semiconductor character, we obtain that the current pattern can be used to distinguish them, suggesting that it can be useful for the development of devices as diagnostics tools for amyloidosislike diseases