Molecular Insights into the Dynamics of Amyloid Fibril Growth: Elongation and Lateral Assembly of GNNQQNY Protofibrils Article Swipe
Torsten John
,
Aldo Rampioni
,
David Poger
,
Alan E. Mark
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1021/acschemneuro.3c00754
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1021/acschemneuro.3c00754
The self-assembly of peptides and proteins into β-sheet rich amyloid fibrils is linked to both functional and pathological states. In this study, the growth of fibrillar structures of the short peptide GNNQQNY, a fragment from the yeast prion Sup35 protein, was examined. Molecular dynamics simulations were used to study alternative mechanisms of fibril growth, including elongation through binding of monomers as well as fibril self-assembly into larger, more mature structures. It was found that after binding, monomers diffused along preformed fibrils toward the ends, supporting the mechanism of fibril growth via elongation. Lateral assembly of protofibrils was found to occur readily, suggesting that this could be the key to transitioning from isolated fibrils to mature multilayer structures. Overall, the work provides mechanistic insights into the competitive pathways that govern amyloid fibril growth.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1021/acschemneuro.3c00754
- OA Status
- green
- Cited By
- 5
- References
- 76
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4390974133
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4390974133Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1021/acschemneuro.3c00754Digital Object Identifier
- Title
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Molecular Insights into the Dynamics of Amyloid Fibril Growth: Elongation and Lateral Assembly of GNNQQNY ProtofibrilsWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2024Year of publication
- Publication date
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2024-01-18Full publication date if available
- Authors
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Torsten John, Aldo Rampioni, David Poger, Alan E. MarkList of authors in order
- Landing page
-
https://doi.org/10.1021/acschemneuro.3c00754Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
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greenOpen access status per OpenAlex
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https://research.rug.nl/en/publications/a5ce26f3-7c42-4d98-839f-9b940ae0e281Direct OA link when available
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Fibril, Elongation, Biophysics, Monomer, Amyloid fibril, Amyloid (mycology), Chemistry, Molecular dynamics, Peptide, Biochemistry, Amyloid β, Biology, Materials science, Ultimate tensile strength, Polymer, Computational chemistry, Inorganic chemistry, Medicine, Pathology, Organic chemistry, Disease, MetallurgyTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
5Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 3, 2024: 2Per-year citation counts (last 5 years)
- References (count)
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76Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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