Revealing molecular-level surface structure of amyloid fibrils in liquid by means of frequency modulation atomic force microscopy.

Fukuma, Takeshi, Mostaert, Anika S, Serpell, Louise C and Jarvis, Suzanne P (2008) Revealing molecular-level surface structure of amyloid fibrils in liquid by means of frequency modulation atomic force microscopy. Nanotechnology, 19 (38). pp. 384010-384016. ISSN 0957-4484

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Abstract

We have investigated the surface structure of islet amyloid polypeptide (IAPP) fibrils and a-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 ß-strands aligned perpendicular to the fibril axis with a spacing of 0.5 nm are resolved in FM-AFM images, which confirms cross-ß 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 a-synuclein protofibrils. However, in contrast to the case for IAPP fibrils, the stripes are oriented 30° from the axis, suggesting the possibility of ß-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.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Depositing User: Louise Serpell
Date Deposited: 06 Feb 2012 19:38
Last Modified: 21 Mar 2012 12:04
URI: http://sro.sussex.ac.uk/id/eprint/21617
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