Oligomerization of amyloid A beta(16-22) peptides using hydrogen bonds and hydrophobicity forces

Summary, in English

The 16 - 22 amino-acid fragment of the beta-amyloid peptide associated with the Alzheimer's disease, Abeta, is capable of forming amyloid fibrils. Here we study the aggregation mechanism of Abeta(16-22) peptides by unbiased thermodynamic simulations at the atomic level for systems of one, three, and six Abeta(16-22) peptides. We find that the isolated Abeta(16-22) peptide is mainly a random coil in the sense that both the alpha-helix and beta-strand contents are low, whereas the three- and six-chain systems form aggregated structures with a high beta-sheet content. Furthermore, in agreement with experiments on Abeta(16-22) fibrils, we find that large parallel beta-sheets are unlikely to form. For the six-chain system, the aggregated structures can have many different shapes, but certain particularly stable shapes can be identified.

• Författare: Giorgio Favrin; Anders Irbäck; Sandipan Mohanty
• Avdelning/ar: Beräkningsbiologi och biologisk fysik - Har omorganiserats; Institutionen för astronomi och teoretisk fysik - Har omorganiserats
• Publiceringsår: 2004
• Språk: Engelska
• Sidor: 3657-3664
• Publikation/Tidskrift/Serie: Biophysical Journal
• Volym: 87
• Issue: 6
• Länkar: http://dx.doi.org/10.1529/biophysj.104.046839
• Dokumenttyp: Artikel i tidskrift
• Förlag: Cell Press
• Ämne: Biophysics
• Status: Published
• ISBN/ISSN/Övrigt: ISSN: 1542-0086