Early amyloid β-protein aggregation precedes conformational change†
Bogdan Barz,Olujide O. Olubiyi
Chemical Communications Pub Date : 01/15/2014 00:00:00 , DOI:10.1039/C3CC48704K
Abstract

The aggregation of amyloid-β protein (1–42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers without significant changes in the internal structure of individual proteins. The aggregation process is characterized in terms of transition networks.

Graphical abstract: Early amyloid β-protein aggregation precedes conformational change