Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecularcCrowding
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
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.
IdentifiersURN: urn:nbn:se:umu:diva-18199DOI: doi:10.1021/ja076059oOAI: oai:DiVA.org:umu-18199DiVA: diva2:157872