Expanding the repertoire of amyloid polymorphs by co-polymerization of related protein precursors

Abstract

Background: Amyloid fibrils in vivo are rarely composed of a single protein, yet the consequences of co-polymerization of different proteins are relatively poorly understood. Results: Fibrils formed by co-polymerizing two variants of β2-microglobulin were characterized alongside their homopolymer equivalents. Conclusion: The three fibril types have different structural and thermodynamic properties. Significance: Co-polymerization of protein precursors enhances the structural and thermodynamic diversity of amyloid fibrils. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.