Autor(es): Carvalho, Tiago ; Pinto, Ricardo J. B. ; Martins, Manuel A. ; Silvestre, Armando J. D. ; Freire, Carmen S. R.
Data: 2016
Identificador Persistente: http://hdl.handle.net/10773/19883
Origem: RIA - Repositório Institucional da Universidade de Aveiro
Assunto(s): THIOFLAVIN T; PROTEIN; FIBRILLATION; POLYMORPHISM; AGGREGATION; MECHANISMS; MORPHOLOGY; NANOWIRES; TOXICITY
Insulin amyloid fibrils with enhanced aspect ratio, were prepared using a timesaving microwave assisted (MW) methodology, reducing the incubation time from 13 to 2 h. The fibrillation process was followed indirectly by Thioflavin T Fluorescence and UV-vis analysis, by measuring the amount of beta-sheets formed and the insulin present in solution, respectively. TEM and AFM analysis revealed that the insulin fibrils obtained through the MW method, have very similar lengths but are much thinner than the ones obtained using the conventional method (CM). Additionally, it was verified that the nature of the peptides present in the final insulin fibrils was not affected by microwave irradiation. These morphological differences might reflect on noticeably enhanced mechanical and optical properties that can exploited on the development of advanced bionanomaterials. (C) 2016 Elsevier B.V. All rights reserved.
