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Review

Nanoimaging for prion related diseases

, , , &
Pages 265-274 | Received 01 Jun 2010, Accepted 23 Jul 2010, Published online: 01 Oct 2010

Figures & data

Figure 1 Scheme illustrating that a protein molecule can adopt several conformational states which may result in aggregates of different morphologies. AFM images of CGNNQQNY peptide from Sup35 yeast prion protein aggregated with the formation of fibrils of distinct morphologies at different conditions. Scale bar is 500 nm.

Figure 1 Scheme illustrating that a protein molecule can adopt several conformational states which may result in aggregates of different morphologies. AFM images of CGNNQQNY peptide from Sup35 yeast prion protein aggregated with the formation of fibrils of distinct morphologies at different conditions. Scale bar is 500 nm.

Figure 2 (A) Sketch of a back reflection TERS setup, (B) TERS spectra of a fibril formed by CGNNQQNY peptide from Sup35 yeast prion protein on adjacent points separated by 7 nm.

Figure 2 (A) Sketch of a back reflection TERS setup, (B) TERS spectra of a fibril formed by CGNNQQNY peptide from Sup35 yeast prion protein on adjacent points separated by 7 nm.

Figure 3 Dynamic force spectrum of CGNNQQNY peptide interactions measured at pH 5.6.

Figure 3 Dynamic force spectrum of CGNNQQNY peptide interactions measured at pH 5.6.

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