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Membrane-mimetic systems for biophysical studies of the amyloid-beta peptide
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42019 (English)In: Biochimica et Biophysica Acta - Proteins and Proteomics, ISSN 1570-9639, E-ISSN 1878-1454, Vol. 1867, no 5, p. 492-501Article in journal (Refereed) Published
Abstract [en]

The interplay between the amyloid-beta (A beta) peptide and cellular membranes have been proposed as an important mechanism for toxicity in Alzheimer's disease (AD). Membrane environments appear to influence A beta aggregation and may stabilize intermediate A beta oligomeric states that are considered to be neurotoxic. One important role for molecular biophysics within the field of A beta studies is to characterize the structure and dynamics of the A beta peptide in various states, as well as the kinetics of transfer between these states. Because biological cell membranes are very complex, simplified membrane models are needed to facilitate studies of A beta and other amyloid proteins in lipid environments. In this review, we examine different membrane-mimetic systems available for molecular studies of A beta. An introduction to each system is given, and examples of important findings are presented for each system. The benefits and drawbacks of each system are discussed from methodical and biological perspectives.

Place, publisher, year, edition, pages
2019. Vol. 1867, no 5, p. 492-501
Keywords [en]
Alzheimer's disease, Amyloid, Protein aggregation, Protein-membrane interaction, Biomembranes, Protein spectroscopy
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-169090DOI: 10.1016/j.bbapap.2018.11.005ISI: 000465154400005PubMedID: 30468884OAI: oai:DiVA.org:su-169090DiVA, id: diva2:1326563
Available from: 2019-06-18 Created: 2019-06-18 Last updated: 2019-06-18Bibliographically approved

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Österlund, NicklasWärmländer, Sebastian K. T. S.Gräslund, Astrid
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