دورية أكاديمية
أعرض في EDS

The role of shear forces in primary and secondary nucleation of amyloid fibrils.

التفاصيل البيبلوغرافية
العنوان: The role of shear forces in primary and secondary nucleation of amyloid fibrils.
المؤلفون: Axell E; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Hu J; Division of Physical Chemistry, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Lindberg M; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Dear AJ; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden.; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, Cambridge University, CB2 1EW Cambridge, United Kingdom., Ortigosa-Pascual L; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Andrzejewska EA; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, Cambridge University, CB2 1EW Cambridge, United Kingdom., Šneiderienė G; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, Cambridge University, CB2 1EW Cambridge, United Kingdom., Thacker D; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Knowles TPJ; Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, Cambridge University, CB2 1EW Cambridge, United Kingdom., Sparr E; Division of Physical Chemistry, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden., Linse S; Biochemistry and Structural Biology, Department of Chemistry, Lund University, SE-221 00 Lund, Sweden.
المصدر: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Jun 18; Vol. 121 (25), pp. e2322572121. Date of Electronic Publication: 2024 Jun 14.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : National Academy of Sciences
مواضيع طبية MeSH: Amyloid*/metabolism , Amyloid*/chemistry, Kinetics ; Humans ; Shear Strength ; Protein Aggregates ; Peptides/chemistry ; Peptides/metabolism ; Alzheimer Disease/metabolism
مستخلص: Shear forces affect self-assembly processes ranging from crystallization to fiber formation. Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides and investigated in detail for A[Formula: see text]42, which is associated with Alzheimer's disease. To gain mechanistic insights into the effect of mild agitation, nonseeded and seeded aggregation reactions were set up at various peptide concentrations with and without an inhibitor. First, an effect on fibril fragmentation was excluded by comparing the monomer-concentration dependence of aggregation kinetics under idle and agitated conditions. Second, using a secondary nucleation inhibitor, Brichos, the agitation effect on primary nucleation was decoupled from secondary nucleation. Third, an effect on secondary nucleation was established in the absence of inhibitor. Fourth, an effect on elongation was excluded by comparing the seeding potency of fibrils formed under idle or agitated conditions. We find that both primary and secondary nucleation steps are accelerated by gentle agitation. The increased shear forces facilitate both the detachment of newly formed aggregates from catalytic surfaces and the rate at which molecules are transported in the bulk solution to encounter nucleation sites on the fibril and other surfaces. Ultrastructural evidence obtained with cryogenic transmission electron microscopy and free-flow electrophoresis in microfluidics devices imply that agitation speeds up the detachment of nucleated species from the fibril surface. Our findings shed light on the aggregation mechanism and the role of detachment for efficient secondary nucleation. The results inform on how to modulate the relative importance of different microscopic steps in drug discovery and investigations.
Competing Interests: Competing interests statement:The authors declare no competing interest.
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معلومات مُعتمدة: 2015-00143 Vetenskapsrådet (VR); 2019-02397 Vetenskapsrådet (VR); NNF19OC0054635 Novo Nordisk Fonden (NNF); 945378 EC | Horizon 2020 Framework Programme (H2020); 10100161 EC | Horizon 2020 Framework Programme (H2020); S02304 UKRI | Engineering and Physical Sciences Research Council (EPSRC)
فهرسة مساهمة: Keywords: acceleration; aggregation; amyloid beta peptide; convection; double nucleation
المشرفين على المادة: 0 (Amyloid)
0 (Protein Aggregates)
0 (Peptides)
تواريخ الأحداث: Date Created: 20240614 Date Completed: 20240614 Latest Revision: 20240626
رمز التحديث: 20240626
مُعرف محوري في PubMed: PMC11194593
DOI: 10.1073/pnas.2322572121
PMID: 38875148
قاعدة البيانات: MEDLINE
الوصف
تدمد:1091-6490
DOI:10.1073/pnas.2322572121