Controlling Amyloid Assembly Dynamics Using Spin Interfaces.

ABSTRACT: Protein aggregation into amyloid fibrils is central to numerous diseases, yet the role of electron spin interactions during nucleation and self-assembly remains unexplored. We investigated amyloid formation of A-β(1-42) polypeptide, implicated in Alzheimer's disease, and its smaller recognition motifs on ferromagnetic substrates. We observed a strong dependence of fibril formation dynamics on the substrate's magnetization orientation using electron and fluorescence microscopy. Specifically, one magnetization orientation yielded approximately twice as many and significantly longer (up to 20-fold) fibrils compared with the opposite orientation, a preference that flipped with the opposite monomer chirality. Furthermore, ATR-FTIR detected structural variations in the fibril structure, dependin

SUBMITTER: Kapon Y 

PROVIDER: S-EPMC12356117 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature