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All-atom Molecular Dynamics Studies of the Full-length β-Amyloid Peptides by Edgar Luttmann; Gregor Fels is a Physics and Astronomy article available to read on EtoBox.

What is All-atom Molecular Dynamics Studies of the Full-length β-Amyloid Peptides about?

b-Amyloid peptides are believed to play an essential role in AlzheimerÕs disease (AD), due to their sedimentation in the form of bamyloid aggregates in the brain of AD-patients, and the in vitro neurotoxicity of oligomeric aggregates. The monomeric peptides come in different lengths of 39-43 residues, of which the 42 alloform seems to be most strongly associated with AD-symptoms. Structural information on these peptides to date comes from NMR studies in acidic solutions, organic solvents, or on shorter fragments of the peptide. In addition X-ray and solid-state NMR investigations of amyloid fibrils yield insight into the structure of the final aggregate and therefore define the endpoint of any conformational change of an Ab-monomer along the aggregation process. The conformational changes necessary to connect the experimentally known conformations are not yet understood and this process is an active field of research. In this paper, we report results from all-atom molecular dynamics simulations based on experimental data from four different peptides of 40 amino acids and two peptides consisting of 42 amino acids. The simulations allow for the analysis of intramolecular interactions

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Author

Edgar Luttmann; Gregor Fels

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0301-0104)

Published

2006

Language

EN

Field

Physics and Astronomy (Physical Sciences)