{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(1)"],"submitter":["Miller A"],"funding":["We gratefully acknowledge funding from the Finlay Scholarship and the Frances and Augustus Newman Foundation."],"pubmed_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 "],"journal":["Communications biology"],"pagination":["153"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10847148"],"repository":["biostudies-literature"],"pubmed_title":["Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils."],"pmcid":["PMC10847148"],"pubmed_authors":["Knowles TPJ","Vendruscolo M","Klimont E","Ruggeri FS","Miller A","Chia S"],"additional_accession":[]},"is_claimable":false,"name":"Maturation-dependent changes in the size, structure and seeding capacity of Aβ42 amyloid fibrils.","description":"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 ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2025-04-05T00:01:46.3Z","creation":"2025-04-05T00:01:46.3Z"},"accession":"S-EPMC10847148","cross_references":{"pubmed":["38321144"],"doi":["10.1038/s42003-024-05858-7"]}}