Structure and dynamics of rare states of the Alzheimer's disease beta-amyloid peptide
| Grant number: | 16/04176-4 |
| Support type: | Regular Research Grants |
| Duration: | June 01, 2016 - May 31, 2018 |
| Field of knowledge: | Physical Sciences and Mathematics - Physics - Condensed Matter Physics |
| Principal Investigator: | Nelson Augusto Alves |
| Grantee: | Nelson Augusto Alves |
| Home Institution: | Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil |
Abstract
Molecular dynamics (MD) simulations will be performed to describe intermediate states of amyloid $\beta$-peptides (A$\beta$) with 40 residues (A$\beta_{40}$), 42 residues (A$\beta_{42}$), and a set of peptides obtained by local mutations in the A$\beta$ sequences. A$\beta$ peptides and their mutant variants play a central role in Alzheimer's disease and present different toxicity and aggregation propensities to convert from their soluble forms into insoluble fibrillar aggregates. The ensemble structures will be obtained from MD simulations using the GROMACS package with an all-atom model. The critical properties of these peptides and the features of the conformational transitions will be addressed to describe the mutation effects on the propensities of these peptides. (AU)