Mechanistic and structural aspects of the interaction of luminescent conjugated polymers with amyloid oligomers
2010 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, Vol. 17, no S1, 98-99 p.Article in journal, Meeting abstract (Other academic) Published
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.
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-60256DOI: 10.3109/13506121003737419ISI: 000279801500115OAI: oai:DiVA.org:liu-60256DiVA: diva2:355797
XII INTERNATIONAL SYMPOSIUM ON AMYLOIDOSIS, 'From Molecular Mechanisms Toward the Cure of Systemic Amyloidoses', Rome, Italy, April 18–21, 2010