ORCID Profile
0000-0003-0726-4183
Current Organisation
Diamond Light Source Ltd
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Publisher: Royal Society of Chemistry (RSC)
Date: 2022
DOI: 10.1039/D2FD90026B
Publisher: American Chemical Society (ACS)
Date: 28-05-2010
DOI: 10.1021/JP101374E
Abstract: 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 beta (Abeta) 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 stalks is used to extract orientational order parameters from the 0.48 nm reflection in the cross-beta pattern, from which an orientational distribution function is obtained. X-ray diffraction on solutions subject to capillary flow confirmed orientation in situ at the level of the cross-beta pattern. The information on fibril and tyrosine orientation from polarized Raman spectroscopy is compared with results from NEXAFS experiments on s les prepared as films on silicon. This indicates fibrils are aligned parallel to the surface, with phenyl ring normals perpendicular to the surface. Possible disulfide bridging leading to peptide dimer formation was excluded by Raman spectroscopy, whereas dityrosine formation was probed by fluorescence experiments and was found not to occur except under alkaline conditions. Congo red binding was found not to influence the cross-beta XRD pattern.
Publisher: Elsevier BV
Date: 05-2009
Publisher: American Chemical Society (ACS)
Date: 28-05-2021
DOI: 10.1021/JACS.1C02859
Publisher: Wiley
Date: 07-2020
Publisher: Wiley
Date: 07-2020
Location: United Kingdom of Great Britain and Northern Ireland
Location: Germany
Location: Germany
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Georg Held.