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Misfolding of amyloidogenic proteins at membrane surfaces:  the impact of macromolecularcCrowding
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2007 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 129, no 48, 14848-14849 p.Article in journal (Refereed) Published
Abstract [en]

The presence of inert macromolecular crowding agents mimics the situation in vivo where amyloidogenic proteins are released into an aqueous, congested intracellular environment. By using the amphiphatic Alzheimer A-protein as the model system, the presence of a three-dimensional macromolecular crowding environment enhanced significantly its misfolding behavior if charged membrane surfaces as two-dimensional aggregation templates were present.

Place, publisher, year, edition, pages
2007. Vol. 129, no 48, 14848-14849 p.
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Chemical Sciences
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URN: urn:nbn:se:umu:diva-18199DOI: doi:10.1021/ja076059oOAI: oai:DiVA.org:umu-18199DiVA: diva2:157872
Available from: 2008-09-26 Created: 2008-09-26 Last updated: 2017-12-14Bibliographically approved

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