The Driving Forces of Peptide Aggregation

Abstract

Protein aggregation can be highly detrimental to organisms, and has been associated with diseases including Alzheimer's, Huntington's, type II diabetes, and transmissible spongiform encephalopathies such as Mad Cow disease. There is no single amino acid sequence responsible for aggregation into amyloid-like structures, but rather a large range of amyloidogenic peptides have been discovered. A fragment of the yeast Sup35 prion, GNNQQNY, has been found to aggregate using a "dry, steric zipper" structure. This study looks at mutants of GNNQQNY in order to elucidate the exact contributions of various amino acids to the aggregation process.