Encapsulation and NMR on an Aggregating Peptide before Fibrillogenesis

摘要

In amyloidosis,peptides aggregate first into soluble oligomers,and then into insoluble protofibrils and fibrils.Soluble aggregates are cytotoxic but difficult to observe directly because they are shortlived and prone to form insoluble fibrils.One approach for studying oligomers structurally would be to encapsulate peptides such that they are prevented from further aggregation into fibrils.Wand and co-workers reported methods for encapsulating an aggregating protein in the aqueous core of reverse micelles in liquid hexane.