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Sökning: WAKA:ref > Inganäs Olle > Nilsson K. Peter R.

  • Resultat 1-4 av 4
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  • Herland, Anna, et al. (författare)
  • Synthesis of a regioregular zwitterionic conjugated oligoelectrolyte, usable as an optical probe for detection of amyloid fibril formation at acidic pH
  • 2005
  • Ingår i: Journal of the American Chemical Society. - 0002-7863. ; 127:7, s. 2317-2323
  • Tidskriftsartikel (refereegranskat)abstract
    • Changes of the optical properties of conjugated polyelectrolytes have been utilized to monitor noncovalent interactions between biomolecules and the conjugated polyelectrolytes in sensor applications. A regioregular, zwitterionic conjugated oligoelectrolyte was synthesized in order to create a probe with a defined set of optical properties and hereby facilitate interpretation of biomolecule−oligoelectrolyte interactions. The synthesized oligoelectrolyte was used at acidic pH as a novel optical probe to detect amyloid fibril formation of bovine insulin and chicken lysozyme. Interaction of the probe with formed amyloid fibrils results in changes of the geometry and the electronic structure of the oligoelectrolyte chains, which were monitored with absorption and emission spectroscopy.
  • Nilsson, K.Peter R., et al. (författare)
  • Conformational transitions in a free amino acid functionalized polythiophene
  • 2003
  • Ingår i: Synthetic metals. - Elsevier. - 0379-6779. ; 135-136, s. 291-292
  • Tidskriftsartikel (refereegranskat)abstract
    • A chiral, 3-substituted polythiophene with an amino acid function shows pH-dependent visible, emission and circular dichroism spectra in buffered aqueous solution. At pH equal to pi of the amino acid, the backbone adopts a non-planar right-handed helical conformation and the polymer chains are separated from each other. Increasing pH leads to a more planar conformation of the backbone and an aggregation of the polymer chains occurs. A lower pH will also lead to a more planar conformation of the backbone, but aggregation of the polymer chains appears to be absent. © 2003 Elsevier Science B.V. All rights reserved.
  • Nilsson, K. Peter R., et al. (författare)
  • Imaging distinct conformational states of amyloid-β fibrils in Alzheimer's disease using novel luminescent probes
  • 2007
  • Ingår i: ACS Chemical Biology. - 1554-8929. ; 2:8, s. 553-560
  • Tidskriftsartikel (refereegranskat)abstract
    • Using luminescent conjugated polyelectrolyte probes (LCPs), we demonstrate the possibility to distinguish amyloid-β 1-42 peptide (Aβ1-42) fibril conformations, by analyzing in vitro generated amyloid fibrils of Aβ1-42 formed under quiescent and agitated conditions. LCPs were then shown to resolve such conformational heterogeneity of amyloid deposits in vivo. A diversity of amyloid deposits depending upon morphology and anatomic location was illustrated with LCPs in frozen ex vivo brain sections from a transgenic mouse model (tg-APPswe) of Alzheimer's disease. Comparative LCP fluorescence showed that compact-core plaques of amyloid β precursor protein transgenic mice were composed of rigid dense amyloid. A more abundant form of amyloid plaque displayed morphology of a compact center with a protruding diffuse exterior. Surprisingly, the compact center of these plaques showed disordered conformations of the fibrils, and the exterior was composed of rigid amyloid protruding from the disordered center. This type of plaque appears to grow from more loosely assembled regions toward solidified amyloid tentacles. This work demonstrates how application of LCPs can prove helpful to monitor aggregate structure of in vivo formed amyloid deposits such as architecture, maturity, and origin.
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