Journal article

Molecular dynamics simulations of a fibrillogenic peptide derived from apolipoprotein C-II

E Sue Legge, Herbert Treutlein, Geoffrey J Howlett, Irene Yarovsky

BIOPHYSICAL CHEMISTRY | ELSEVIER SCIENCE BV | Published : 2007

Abstract

The pathway to amyloid fibril formation in proteins involves specific structural changes leading to the combination of misfolded intermediates into oligomeric assemblies. Recent NMR studies showed the presence of "turns" in amyloid peptides, indicating that turn formation may play an important role in the nucleation of the intramolecular folding and possible assembly of amyloid. Fully solvated all-atom molecular dynamics simulations were used to study the structure and dynamics of the apolipoprotein C-II peptide 56 to 76, associated with the formation of amyloid fibrils. The peptide populated an ensemble of turn structures, stabilized by hydrogen bonds and hydrophobic interactions enabling t..

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