Structural Interconversion in Alzheimer's Amyloid-beta(16-35) Peptide in an Aqueous Solution

Autor(es)

Alves, Nelson A. ^[1] ; Frigori, Rafael B. ^[2]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, FFCLRP, Dept Fis, Ave Bandeirantes 3900, BR-14040901 Ribeirao Preto, SP - Brazil

^[2] Univ Tecnol Fed Parana, Rua Cristo Rei 19, BR-85902490 Toledo, PR - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Physical Chemistry B; v. 122, n. 6, p. 1869-1875, FEB 15 2018.
• Citações Web of Science: 3

Resumo

Structural properties of A beta(16-35) fragment are investigated as a model for the amyloid-beta peptide excluding its coil-inducing terminals. Our replica-exchange molecular dynamics simulations using all-atom and explicit aqueous solvation widely reduce any structural bias. The principal folding pathway shows direct conversion of coil to beta-sheet, without the long proposed helix intermediates. Our principal component analysis indicates that the fragment is also intrinsically disordered, as the full amyloid-beta peptide. Thus, the observed folding mechanism lacks free-energy barriers and any peaks in the thermal capacity. (AU)

• Processo FAPESP: 16/04176-4 - Análise sistemática in silico do comportamento crítico do peptídeo amiloide beta e de alguns dos seus mutantes
• Beneficiário: Nelson Augusto Alves
• Modalidade de apoio: Auxílio à Pesquisa - Regular