Protein misfolding and subsequent self-association are complex, intertwined processes, resulting in development of a heterogeneous population of aggregates closely related to many chronic pathological conditions including Type 2 Diabetes Mellitus and Alzheimer’s disease. To address this issue, here, we develop a theoretical model in the general framework of linear stability analysis. According to this model, self-assemblies of peptides with pronounced conformational flexibility may become, under particular conditions, unstable and spontaneously evolve toward an alternating array of partially ordered and disordered monomers.
Carmelo La Rosa, Marcello Condorelli, Giuseppe Compagnini, Fabio Lolicato, Danilo Milardi, Trang Nhu Do, Mikko Karttunen, Martina Pannuzzo, Ayyalusamy Ramamoorthy, Franca Fraternali, Francesca Collu, Human Rezaei, Birgit Strodel & Antonio Raudino