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Self-assembled peptide nanostructures: synthesis, characterization and interaction with model membrane systems

Grant number: 14/12567-8
Support Opportunities:Scholarships in Brazil - Post-Doctorate
Effective date (Start): November 01, 2014
Effective date (End): April 30, 2019
Field of knowledge:Physical Sciences and Mathematics - Physics
Acordo de Cooperação: Coordination of Improvement of Higher Education Personnel (CAPES)
Principal Investigator:Osvaldo Novais de Oliveira Junior
Grantee:Bianca Sandrino
Host Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:13/14262-7 - Nanostructured films from biologically-relevant materials, AP.TEM
Associated scholarship(s):15/23903-1 - Complex Peptide-nanoparticles: preparation, characterization and antitumor activity, BE.EP.PD


The aim of this project is to investigate the interaction between peptides which present the ability of self-assembling with systems that mimic the biomembrane. Among these peptides, two classes were selected, due to their huge biotechnological relevance: peptide nanotubes and peptides involved in the formation of aggregates related with neurodegenerative diseases. Peptide nanotubes are structures formed by the self-assembly of a cyclic peptide, resulting in a tubular architecture. These structures are able to incorporate into the membrane, forming ionic channels. We intend to evaluate the formation of these channels as well as their incorporation by using biomembrane model systems. As mentioned, peptides that aggregate resulting in senile plaques and filaments will be also studied in this project. These aggregates are commonly related to neurodegenerative diseases, such as Alzheimer's disease, Bovine spongiform encephalopathy (mad-cow disease) and Huntington's disease. The experiments will focus on the evaluation of the effects from the interaction with the membrane, and their consequences over the formation of the aggregates. With this purpose, peptides equivalent to the region passive of aggregation in some proteins will be synthesized, such as A -amyloid, prions and Huntington proteins, respectively related with the diseases cited above. This project, in addition to being focused on fundamental aspects among the interaction between peptides and membrane model systems, presents a technological character, since the understanding of these process is strictly related with drug development. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
SANDRINO, B.; JOCHELAVICIUS, K.; VOLPATI, D.; BARBOSA, S. C.; NOBRE, T. M.; OLIVEIRA, JR., O. N.. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract. Chemistry and Physics of Lipids, v. 230, . (13/14262-7, 14/12567-8)

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