ORCID Profile
0000-0002-4549-0926
Current Organisation
University of Reading
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Publisher: American Chemical Society (ACS)
Date: 07-08-2012
DOI: 10.1021/BM3007117
Abstract: A strategy is presented that exploits the ability of synthetic polymers of different nature to disturb the strong self-assembly capabilities of amyloid based β-sheet forming peptides. Following a convergent approach, the peptides of interest were synthesized via solid-phase peptide synthesis (SPPS) and the polymers via reversible addition-fragmentation chain transfer (RAFT) polymerization, followed by a copper(I) catalyzed azide-alkyne cycloaddition (CuAAC) to generate the desired peptide-polymer conjugates. This study focuses on a modified version of the core sequence of the β-amyloid peptide (Aβ), Aβ(16-20) (KLVFF). The influence of attaching short poly(N-isopropylacrylamide) and poly(hydroxyethylacrylate) to the peptide sequences on the self-assembly properties of the hybrid materials were studied via infrared spectroscopy, TEM, circular dichroism and SAXS. The findings indicate that attaching these polymers disturbs the strong self-assembly properties of the biomolecules to a certain degree and permits to influence the aggregation of the peptides based on their β-sheets forming abilities. This study presents an innovative route toward targeted and controlled assembly of amyloid-like fibers to drive the formation of polymeric nanomaterials.
Publisher: American Chemical Society (ACS)
Date: 13-09-2010
DOI: 10.1021/MA101093F
Publisher: Royal Society of Chemistry (RSC)
Date: 2017
DOI: 10.1039/C7NR03263C
Abstract: Upon changing the position, nature and number of the halogen atoms, the same amyloidogenic peptide self-assembles into different nanostructures.
Publisher: Elsevier BV
Date: 03-2007
Publisher: Royal Society of Chemistry (RSC)
Date: 2020
DOI: 10.1039/C9CS00199A
Abstract: Amyloid diseases are global epidemics with profound health, social and economic implications and yet remain without a cure.
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: American Chemical Society (ACS)
Date: 19-06-2018
Publisher: Royal Society of Chemistry (RSC)
Date: 2018
DOI: 10.1039/C7PY01953J
Abstract: Sequence defined peptide–peptoid hybrids create new opportunities for self-assembled nano-structures.
Publisher: Wiley
Date: 29-09-2006
Publisher: Royal Society of Chemistry (RSC)
Date: 2013
DOI: 10.1039/C3RA41979G
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Ian Hamley.