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Superresolution Imaging of Amyloid Fibrils with Binding-Activated Probes
EMBL Heidelberg, Germany .
University of Zurich, Switzerland .
ETH, Switzerland .
University of Zurich, Switzerland .
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2013 (Engelska)Ingår i: ACS Chemical Neuroscience, ISSN 1948-7193, E-ISSN 1948-7193, Vol. 4, nr 7, s. 1057-1061Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Protein misfolding into amyloid-like aggregates underlies many neurodegenerative diseases. Thus, insights into the structure and function of these amyloids will provide valuable information on the pathological mechanisms involved and aid in the design of improved drugs for treating amyloid-based disorders. However, determining the structure of endogenous amyloids at high resolution has been difficult. Here we employ binding-activated localization microscopy (BALM) to acquire superresolution images of alpha-synuclein amyloid fibrils with unprecedented optical resolution. We propose that BALM imaging can be extended to study the structure of other amyloids, for differential diagnosis of amyloid-related diseases and for discovery of drugs that perturb amyloid structure for therapy.

Ort, förlag, år, upplaga, sidor
American Chemical Society , 2013. Vol. 4, nr 7, s. 1057-1061
Nyckelord [en]
Alzheimers disease, Parkinsons disease, amyloid, superresolution, neurodegenerative diseases, binding-activated, localization microscopy, diagnosis, alpha-synuclein
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URN: urn:nbn:se:liu:diva-96720DOI: 10.1021/cn400091mISI: 000322103700005OAI: oai:DiVA.org:liu-96720DiVA, id: diva2:642961
Anmärkning

Funding Agencies|Velux Foundation||Swiss National Science Foundation||Synapsis foundation||Baugarten Stiftung||Bangerter Stiftung grant||Marie Curie Intra-European Fellowship||NCCR Neural Plasticity and Repair||Holcim Fellowship||

Tillgänglig från: 2013-08-23 Skapad: 2013-08-23 Senast uppdaterad: 2017-12-06

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Nilsson, Peter

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