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Dynamics of oligome...
Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide
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- Michaels, Thomas C.T. (author)
- University of Cambridge,Harvard University
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- Šarić, Andela (author)
- University College London
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- Curk, Samo (author)
- University of Maribor,University College London
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- Bernfur, Katja (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Arosio, Paolo (author)
- ETH Zürich
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- Meisl, Georg (author)
- University of Cambridge
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- Dear, Alexander J. (author)
- Harvard University,University of Cambridge
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- Cohen, Samuel I.A. (author)
- University of Cambridge
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- Dobson, Christopher M. (author)
- University of Cambridge
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- Vendruscolo, Michele (author)
- University of Cambridge
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- Linse, Sara (author)
- Lund University,Lunds universitet,NanoLund: Centre for Nanoscience,Annan verksamhet, LTH,Lunds Tekniska Högskola,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Other operations, LTH,Faculty of Engineering, LTH,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Knowles, Tuomas P.J. (author)
- University of Cambridge
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(creator_code:org_t)
- 2020-04-13
- 2020
- English 7 s.
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In: Nature Chemistry. - : Springer Science and Business Media LLC. - 1755-4330 .- 1755-4349. ; 12:5, s. 445-451
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Abstract
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- Oligomeric species populated during the aggregation of the Aβ42 peptide have been identified as potent cytotoxins linked to Alzheimer’s disease, but the fundamental molecular pathways that control their dynamics have yet to be elucidated. By developing a general approach that combines theory, experiment and simulation, we reveal, in molecular detail, the mechanisms of Aβ42 oligomer dynamics during amyloid fibril formation. Even though all mature amyloid fibrils must originate as oligomers, we found that most Aβ42 oligomers dissociate into their monomeric precursors without forming new fibrils. Only a minority of oligomers converts into fibrillar structures. Moreover, the heterogeneous ensemble of oligomeric species interconverts on timescales comparable to those of aggregation. Our results identify fundamentally new steps that could be targeted by therapeutic interventions designed to combat protein misfolding diseases. [Figure not available: see fulltext.].
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Läkemedelskemi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Medicinal Chemistry (hsv//eng)
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- art (subject category)
- ref (subject category)
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- By the author/editor
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Michaels, Thomas ...
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Šarić, Andela
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Curk, Samo
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Bernfur, Katja
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Arosio, Paolo
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Meisl, Georg
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show more...
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Dear, Alexander ...
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Cohen, Samuel I. ...
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Dobson, Christop ...
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Vendruscolo, Mic ...
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Linse, Sara
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Knowles, Tuomas ...
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- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Medicinal Chemis ...
- Articles in the publication
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Nature Chemistry
- By the university
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Lund University