作者
Ian W Hamley, Valeria Castelletto, Claire M Moulton, José Rodríguez-Pérez, Adam M Squires, Tugce Eralp, Georg Held, Matthew R Hicks, Alison Rodger
发表日期
2010/6/24
期刊
The Journal of Physical Chemistry B
卷号
114
期号
24
页码范围
8244-8254
出版商
American Chemical Society
简介
The alignment of model amyloid peptide YYKLVFFC is investigated in bulk and at a solid surface using a range of spectroscopic methods employing polarized radiation. The peptide is based on a core sequence of the amyloid β (Aβ) peptide, KLVFF. The attached tyrosine and cysteine units are exploited to yield information on alignment and possible formation of disulfide or dityrosine links. Polarized Raman spectroscopy on aligned stalks provides information on tyrosine orientation, which complements data from linear dichroism (LD) on aqueous solutions subjected to shear in a Couette cell. LD provides a detailed picture of alignment of peptide strands and aromatic residues and was also used to probe the kinetics of self-assembly. This suggests initial association of phenylalanine residues, followed by subsequent registry of strands and orientation of tyrosine residues. X-ray diffraction (XRD) data from aligned …
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IW Hamley, V Castelletto, CM Moulton… - The Journal of Physical Chemistry B, 2010