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