@article{oai:kanazawa-u.repo.nii.ac.jp:00039997,
 author = {福間, 剛士 and Fukuma, Takeshi and Mostaert, Anika S. and Serpell, Louise C. and Jarvis, Suzanne P.},
 issue = {38},
 journal = {Nanotechnology},
 month = {Sep},
 note = {We have investigated the surface structure of islet amyloid polypeptide (IAPP) fibrils and α-synuclein protofibrils in liquid by means of frequency modulation atomic force microscopy (FM-AFM). Ångström- resolution FM-AFM imaging of isolated macromolecules in liquid is demonstrated for the first time. Individual β-strands aligned perpendicular to the fibril axis with a spacing of 0.5 nm are resolved in FM-AFM images, which confirms cross-β structure of IAPP fibrils in real space. FM-AFM images also reveal the existence of 4 nm periodic domains along the axis of IAPP fibrils. Stripe features with 0.5 nm spacing are also found in images of α-synuclein protofibrils. However, in contrast to the case for IAPP fibrils, the stripes are oriented 30° from the axis, suggesting the possibility of β-strand alignment in protofibrils different from that in mature fibrils or the regular arrangement of thioflavin T molecules present during the fibril preparation aligned at the surface of the protofibrils. © IOP Publishing Ltd., 金沢大学フロンティアサイエンス機構},
 title = {Revealing molecular-level surface structure of amyloid fibrils in liquid by means of frequency modulation atomic force microscopy},
 volume = {19},
 year = {2008}
}