Alzheimer's disease starts with the aggregation of β-amyloid peptides overproduced in the brain. The pathognomic plaques contain 50-100 peptides in parallel and/or antiparallel β-pleated sheet structure. Short peptide fragments called β-sheet breaker (BSB) peptides can bind specifically to β-amyloid peptides hindering the association and aggregation. The 3D structures of the molecular associates between βA6-34 and BSB peptides (Soto's LPFFD, Tjernberg's KLVFF and two new ones) were calculated theoretically by AMBER force field based docking algorithms. The calculated structures emphasize the directing effect and pivotal role of electrostatic forces and the importance of the hydrophobic interactions of the side-chains in binding of BSB peptides to the β-amyloid peptide.
- Amyloid βA(1-42)
- β-Sheet breaker (BSB) peptides
ASJC Scopus subject areas
- Condensed Matter Physics
- Physical and Theoretical Chemistry