Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.

ABSTRACT: Many proteins self-assemble to form amyloid fibrils, which are highly organized structures stabilized by a characteristic cross-β network of hydrogen bonds. This process underlies a variety of human diseases and can be exploited to develop versatile functional biomaterials. Thus, protein self-assembly has been widely studied to shed light on the properties of fibrils and their intermediates. A still open question in the field concerns the microscopic processes that underlie the long-time behaviour and properties of amyloid fibrillar assemblies. Here, we use atomic force microscopy with angstrom-sensitivity to observe that amyloid fibrils undergo a maturation process, associated with an increase in both fibril length and thickness, leading to a decrease of their density, and to a change in

SUBMITTER: Miller A 

PROVIDER: S-EPMC10847148 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature