Generation of Electrochemical Gradient from Peptide Self-Assembly

Abstract

The nucleating core of the Amyloid β peptide associated with Alzheimer's disease is able to organize into a peptide bilayer maintaining dimensions similar to biological phospholipid membranes. However, the dynamics of the hydrogen-bonded peptides are certainly different from the flexible alkanes of the lipid membranes, and this crystallinity prompted us to consider their dynamics and functional potential. Here we will review these unique surfaces built on cross-β structures of amyloid, and extend that pattern to mixing of positively- and negatively-charged surfaces to give even higher order architectures with high electrochemical potential across the 4 nm membrane. Further, we have developed EFM analyses to map the charge distribution and explored novel energy or electron transduction reactions. Our results show that these peptide membrane scaffolds are dynamic, and their ability to self-organize offers a new opportunity for engineering specific molecular recognition elements into the peptide assemblies and well-ordered materials.