Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils Academic Article uri icon

abstract

  • The self-assembly of two similar amphiphilic peptides into fibril structures is described. Molecular dynamic simulations show that both can organize similarly in a monolayer, but in the fibril bilayer, one prefers a single organization while the other forms two conformational variants. This assembly difference correlates well with our experimental results.

publication date

  • January 1, 2013