دورية أكاديمية
أعرض في EDS

Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.

التفاصيل البيبلوغرافية
العنوان: Aβ Oligomer Dissociation Is Catalyzed by Fibril Surfaces.
المؤلفون: Dear AJ; Biochemistry and Structural Biology, Lund University, Lund 221 00, Sweden.; Centre for Misfolding Diseases Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., Thacker D; Biochemistry and Structural Biology, Lund University, Lund 221 00, Sweden., Wennmalm S; Department of Applied Physics, Biophysics Group, SciLifeLab, Royal Institute of Technology-KTH, Solna 171 65, Sweden., Ortigosa-Pascual L; Biochemistry and Structural Biology, Lund University, Lund 221 00, Sweden., Andrzejewska EA; Centre for Misfolding Diseases Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., Meisl G; Centre for Misfolding Diseases Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K., Linse S; Biochemistry and Structural Biology, Lund University, Lund 221 00, Sweden., Knowles TPJ; Centre for Misfolding Diseases Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, U.K.; Cavendish Laboratory, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, U.K.
المصدر: ACS chemical neuroscience [ACS Chem Neurosci] 2024 Jun 05; Vol. 15 (11), pp. 2296-2307. Date of Electronic Publication: 2024 May 24.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101525337 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1948-7193 (Electronic) Linking ISSN: 19487193 NLM ISO Abbreviation: ACS Chem Neurosci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society
مواضيع طبية MeSH: Amyloid beta-Peptides*/metabolism , Amyloid beta-Peptides*/chemistry , Peptide Fragments*/chemistry , Peptide Fragments*/metabolism, Humans ; Amyloid/metabolism ; Amyloid/chemistry ; Alzheimer Disease/metabolism ; Kinetics
مستخلص: Oligomeric assemblies consisting of only a few protein subunits are key species in the cytotoxicity of neurodegenerative disorders, such as Alzheimer's and Parkinson's diseases. Their lifetime in solution and abundance, governed by the balance of their sources and sinks, are thus important determinants of disease. While significant advances have been made in elucidating the processes that govern oligomer production, the mechanisms behind their dissociation are still poorly understood. Here, we use chemical kinetic modeling to determine the fate of oligomers formed in vitro and discuss the implications for their abundance in vivo. We discover that oligomeric species formed predominantly on fibril surfaces, a broad class which includes the bulk of oligomers formed by the key Alzheimer's disease-associated Aβ peptides, also dissociate overwhelmingly on fibril surfaces, not in solution as had previously been assumed. We monitor this "secondary nucleation in reverse" by measuring the dissociation of Aβ42 oligomers in the presence and absence of fibrils via two distinct experimental methods. Our findings imply that drugs that bind fibril surfaces to inhibit oligomer formation may also inhibit their dissociation, with important implications for rational design of therapeutic strategies for Alzheimer's and other amyloid diseases.
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معلومات مُعتمدة: International ERC_ European Research Council
فهرسة مساهمة: Keywords: Alzheimer’s; dissociation; fibrils; inhibitor; kinetics; oligomer; therapeutic
المشرفين على المادة: 0 (Amyloid beta-Peptides)
0 (Peptide Fragments)
0 (Amyloid)
0 (amyloid beta-protein (1-42))
تواريخ الأحداث: Date Created: 20240524 Date Completed: 20240605 Latest Revision: 20240709
رمز التحديث: 20240709
مُعرف محوري في PubMed: PMC11157482
DOI: 10.1021/acschemneuro.4c00127
PMID: 38785363
قاعدة البيانات: MEDLINE
الوصف
تدمد:1948-7193
DOI:10.1021/acschemneuro.4c00127