title: Atomic force microscopy of ex vivo amyloid fibrils.
abstract: Here, we report a study of ex vivo amyloid fibrils formed, respectively, by the Leu174Ser Apolipoprotein A-I (ApoA-I-LS) variant and by β2-microglobulin (β2-m) (Relini et al., J. Biol. Chem. 281:16521-16529, 2006; Relini et al., Biochim. Biophys. Acta 1690:33-41, 2004). In the work on ApoA-I-LS, the AFM has been used to characterize and compare the morphologies of amyloid fibrils isolated from two different patients, while in the study on β2-m our investigation provided important information about the factors that can promote the aggregation in vivo.
authors.affiliation: Nanophysics Unit, Italian Institute of Technology, Via Morego 30, 16163 Genova, Italy. claudio.canale@iit.it
authors.forename: Claudio
authors.initials: C
authors.lastname: Canale
authors.forename: Annalisa
authors.initials: A
authors.lastname: Relini
authors.forename: Alessandra
authors.initials: A
authors.lastname: Gliozzi
mesh_terms: D000538:Aluminum Silicates / Q000737:chemistry; D000682:Amyloid / Q000302:isolation & purification / Q000648:ultrastructure*; D001053:Apolipoproteins / Q000302:isolation & purification / Q000648:ultrastructure; D006801:Humans; D018625:Microscopy, Atomic Force; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000648:ultrastructure; D013499:Surface Properties; D001613:beta 2-Microglobulin / Q000737:chemistry / Q000302:isolation & purification / Q000648:ultrastructure
chemical_list: D000538:Aluminum Silicates; D000682:Amyloid; D001053:Apolipoproteins; D011994:Recombinant Proteins; D001613:beta 2-Microglobulin; C011934:mica