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Mechanistic and structural aspects of the interaction of luminescent conjugated polymers with amyloid oligomers
Institute of Neuropathology, University Hospital Zurich, Zu¨ rich, Switzerland.
Institute of Neuropathology, University Hospital Zurich, Zu¨ rich, Switzerland.
Institute of Neuropathology, University Hospital Zurich, Zu¨ rich, Switzerland.
Institute of Molecular Biology and Biophysics, Swiss Federal Institute of Technology, Zürich, Switzerland.
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2010 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 17, no S1, 98-99 p.Article in journal, Meeting abstract (Other academic) Published
Abstract [en]

Protein  misfolding  and aggregation  diseases, such as e.g. Alzheimer’s disease, are associated by the accumulation of a disease-related protein.  The pathogenic  mechanisms involved in these confor- mational diseases are only poorly understood. Luminescent-conjugated   polymers    (LCPs)     have been   shown   as  a  sensitive   tool   for  detection   of amyloid deposits. In contrast to commonly used amyloidotropic  dyes  such  as  thioflavins  or  Congo Red, LCPs are composed of flexible polythiophene chains which allow rotation  of the molecule.  Upon binding to amyloids, the LCPs alter their spectral properties  in a conformation dependent manner. However,  there  is still limited  information available on the binding  mechanism and binding  properties  of the LCPs  to amyloid fibrils and oligomers.

We  have  produced  recombinant  human   Aβ1-42 (recAβ1-42) protein  in Escherichia coli and  purified it by conventional chromatographic techniques in large  quantities. The  recAβ-protein was  incubated in the presence  of SDS to induce formation  of homogenous, globular Aβ-oligomers  with a size of approximately   60  kDa,  known  as  Aβ-globulomers. We present  first biophysical  and  spectroscopic data used  to study  the  binding  and  structural properties of  the  complex   formed   by  the  globulomers   and LCPs  with various  charged  side chains.  These  data will  provide   a  more   detailed   knowledge   of  the binding    mode    of   amyloidogenic    probes    which is essential for understanding the structural char- acteristics    of   amyloid   fibrils   detected    by   thesemolecules.

Place, publisher, year, edition, pages
Informa Healthcare, 2010. Vol. 17, no S1, 98-99 p.
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Engineering and Technology
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URN: urn:nbn:se:liu:diva-60256DOI: 10.3109/13506121003737419ISI: 000279801500115OAI: oai:DiVA.org:liu-60256DiVA: diva2:355797
Conference
XII INTERNATIONAL SYMPOSIUM ON AMYLOIDOSIS, 'From Molecular Mechanisms Toward the Cure of Systemic Amyloidoses', Rome, Italy, April 18–21, 2010
Available from: 2010-10-08 Created: 2010-10-08 Last updated: 2017-12-12Bibliographically approved

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Nilsson, Peter

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