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Conformational Switching in PolyGln Amyloid Fibrils Resulting from a Single Amino Acid Insertion
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland.
Laboratory of Structural Biology, National Institute of Arthritis, Musculoskeletal, and Skin Diseases, National Institutes of Health, Bethesda, Maryland.
Centre de Recherches de Biochimie Macromoléculaire, CNRS, University of Montpellier 1 and 2.
Centre de Recherches de Biochimie Macromoléculaire, CNRS, University of Montpellier 1 and 2.
Vise andre og tillknytning
2014 (engelsk)Inngår i: Biophysical Journal, ISSN 0006-3495, E-ISSN 1542-0086, Vol. 106, nr 10, s. 2134-2142Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The established correlation between neurodegenerative disorders and intracerebral deposition of polyglutamine aggregates motivates attempts to better understand their fibrillar structure. We designed polyglutamines with a few lysines inserted to overcome the hindrance of extreme insolubility and two D-lysines to limit the lengths of β-strands. One is 33 amino acids long (PolyQKd-33) and the other has one fewer glutamine (PolyQKd-32). Both form well-dispersed fibrils suitable for analysis by electron microscopy. Electron diffraction confirmed cross-β structures in both fibrils. Remarkably, the deletion of just one glutamine residue from the middle of the peptide leads to substantially different amyloid structures. PolyQKd-32 fibrils are consistently 10–20% wider than PolyQKd-33, as measured by negative staining, cryo-electron microscopy, and scanning transmission electron microscopy. Scanning transmission electron microscopy analysis revealed that the PolyQKd-32 fibrils have 50% higher mass-per-length than PolyQKd-33. This distinction can be explained by a superpleated β-structure model for PolyQKd-33 and a model with two β-solenoid protofibrils for PolyQKd-32. These data provide evidence for β-arch-containing structures in polyglutamine fibrils and open future possibilities for structure-based drug design.

sted, utgiver, år, opplag, sider
2014. Vol. 106, nr 10, s. 2134-2142
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URN: urn:nbn:se:ltu:diva-3196DOI: 10.1016/j.bpj.2014.03.047Lokal ID: 0fd7d673-773e-4079-a8e7-f810580b537fOAI: oai:DiVA.org:ltu-3196DiVA, id: diva2:976052
Merknad
Validerad; 2014; 20140527 (andbra)Tilgjengelig fra: 2016-09-29 Laget: 2016-09-29 Sist oppdatert: 2017-11-24bibliografisk kontrollert

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