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Structural evolution and membrane interactions of Alzheimer's amyloid‐beta peptide oligomers: New knowledge from single‐molecule fluorescence studies
dc.contributor.authorJohnson, Robin D.en_US
dc.contributor.authorSteel, Duncan G.en_US
dc.contributor.authorGafni, Arien_US
dc.date.accessioned2014-07-03T14:41:12Z
dc.date.availableWITHHELD_13_MONTHSen_US
dc.date.available2014-07-03T14:41:12Z
dc.date.issued2014-07en_US
dc.identifier.citationJohnson, Robin D.; Steel, Duncan G.; Gafni, Ari (2014). "Structural evolution and membrane interactions of Alzheimer's amyloid‐beta peptide oligomers: New knowledge from single‐molecule fluorescence studies." Protein Science 23(7): 869-883.en_US
dc.identifier.issn0961-8368en_US
dc.identifier.issn1469-896Xen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/107477
dc.description.abstractAmyloid‐β peptide (Aβ) oligomers may represent the proximal neurotoxin in Alzheimer's disease. Single‐molecule microscopy (SMM) techniques have recently emerged as a method for overcoming the innate difficulties of working with amyloid‐β, including the peptide's low endogenous concentrations, the dynamic nature of its oligomeric states, and its heterogeneous and complex membrane interactions. SMM techniques have revealed that small oligomers of the peptide bind to model membranes and cells at low nanomolar‐to‐picomolar concentrations and diffuse at rates dependent on the membrane characteristics. These methods have also shown that oligomers grow or dissociate based on the presence of specific inhibitors or promoters and on the ratio of Aβ40 to Aβ42. Here, we discuss several types of single‐molecule imaging that have been applied to the study of Aβ oligomers and their membrane interactions. We also summarize some of the recent insights SMM has provided into oligomer behavior in solution, on planar lipid membranes, and on living cell membranes. A brief overview of the current limitations of the technique, including the lack of sensitive assays for Aβ‐induced toxicity, is included in hopes of inspiring future development in this area of research.en_US
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherAmyloid‐Beta Peptideen_US
dc.subject.otherOligomersen_US
dc.subject.otherSingle‐Molecule Microscopyen_US
dc.subject.otherFluorescenceen_US
dc.subject.otherPeptide‐Membrane Interactionen_US
dc.subject.otherAlzheimer's Diseaseen_US
dc.titleStructural evolution and membrane interactions of Alzheimer's amyloid‐beta peptide oligomers: New knowledge from single‐molecule fluorescence studiesen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/107477/1/pro2479.pdf
dc.identifier.doi10.1002/pro.2479en_US
dc.identifier.sourceProtein Scienceen_US
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dc.owningcollnameInterdisciplinary and Peer-Reviewed


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