Amyloid Peptide Channels

Abstract

Amyloid peptides and proteins appear to play a pathophysiologic role in amyloid diseases. Many amyloid peptides have been found to form ion channels under physiologic conditions. The channels from various diseases share common properties including heterodispersity, irreversibility, weak ionic selectivity, voltage-independent inhibition by Congo red and blockade by Zn+2. These features would make these channels likely to depolarize target cells and mitochondria, disrupt Ca+2 regulation, and deplete cellular energy stores leading to cell dysfunction and death. The failure of many anti-amyloid drugs in human clinical trials may be related to the membrane location of amyloid channels.