Intermolecular crosslinking of abnormal prion protein is efficiently induced by a primuline-sensitized photoreaction

Half a century of amyloids: past, present and future

“…Other protocols relied on the use of chemical or radical-mediated crosslinking approaches to trap and/or stabilize transient oligomers to facilitate their characterization or isolation. [180][181][182][183][184][185][186] At the structural level, on-pathway oligomers tend to exhibit a mixture of secondary structure contents, [187][188][189] often dominated by b-sheet conformations. 190 Compared to amyloid fibrils, oligomeric intermediates of most amyloid forming proteins exhibit weak binding to the amyloid specific dyes thioflavin T/S (ThT/S) and Congo red, 191,192 suggesting that they have not acquired the cross-b structure that is characteristic of amyloid fibrils, although studies on Ab oligomers using X-ray fiber diffraction have suggested that some oligomers possess cross-b-like conformations.…”