Infrared linear dichroism spectroscopy on amyloid ﬁbrils aligned by molecular combing
Rodriguez-Perez, J. C., Hamley, I. W. and Squires, A. M. (2011) Infrared linear dichroism spectroscopy on amyloid ﬁbrils aligned by molecular combing. Biomacromolecules, 12 (5). pp. 1810-1821. ISSN 1525-7797
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To link to this article DOI: 10.1021/bm200167n
We report the use of molecular combing as an alignment method to obtain macroscopically oriented amyloid fibrils on planar surfaces. The aligned fibrils are studied by polarized infrared spectroscopy. This gives structural information that cannot be definitively obtained from standard infrared experiments on isotropic samples, for example, confirmation of the characteristic cross-beta amyloid core structure, the side-chain orientation from specific amino acids, and the arrangement of the strands within the fibrils, as we demonstrate here. We employed amyloid fibrils from hen egg white lysozyme (HEWL) and from a model octapeptide. Our results demonstrate molecular combing as a straightforward method to align amyloid fibrils, producing highly anisotropic infrared linear dichroism (IRLD) spectra.