Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design Article Swipe
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· 2017
· Open Access
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· DOI: https://doi.org/10.1098/rsfs.2016.0160
Amyloid nanofibrils are ubiquitous biological protein fibrous aggregates, with a wide range of either toxic or beneficial activities that are relevant to human disease and normal biology. Protein amyloid fibrillization occurs via nucleated polymerization, through non-covalent interactions. As such, protein nanofibril formation is based on a complex interplay between kinetic and thermodynamic factors. The process entails metastable oligomeric species and a highly thermodynamically favoured end state. The kinetics, and the reaction pathway itself, can be influenced by third party moieties, either molecules or surfaces. Specifically, in the biological context, different classes of biomolecules are known to act as catalysts, inhibitors or modifiers of the generic protein fibrillization process. The biological aggregation modifiers reviewed here include lipid membranes of varying composition, glycosaminoglycans and metal ions, with a final word on xenobiotic compounds. The corresponding molecular interactions are critically analysed and placed in the context of the mechanisms of cytotoxicity of the amyloids involved in diverse pathologies and the non-toxicity of functional amyloids (at least towards their biological host). Finally, the utilization of this knowledge towards the design of bio-inspired and biocompatible nanomaterials is explored.
Related Topics
- Type
- review
- Language
- en
- Landing Page
- https://doi.org/10.1098/rsfs.2016.0160
- OA Status
- green
- Cited By
- 30
- References
- 177
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2624790550
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2624790550Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1098/rsfs.2016.0160Digital Object Identifier
- Title
-
Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial designWork title
- Type
-
reviewOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2017Year of publication
- Publication date
-
2017-06-16Full publication date if available
- Authors
-
Durga Dharmadana, Nicholas P. Reynolds, Charlotte E. Conn, Céline ValéryList of authors in order
- Landing page
-
https://doi.org/10.1098/rsfs.2016.0160Publisher landing page
- Open access
-
YesWhether a free full text is available
- OA status
-
greenOpen access status per OpenAlex
- OA URL
-
https://www.ncbi.nlm.nih.gov/pmc/articles/5474041Direct OA link when available
- Concepts
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Context (archaeology), Chemistry, Biomolecule, Amyloid (mycology), Amyloid disease, Biocompatible material, Cytotoxicity, Biomaterial, Biophysics, Nanotechnology, Amyloid fibril, Biochemistry, Materials science, In vitro, Biology, Amyloid β, Organic chemistry, Paleontology, Medicine, Disease, Pathology, Biomedical engineering, Inorganic chemistryTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
30Total citation count in OpenAlex
- Citations by year (recent)
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2024: 3, 2023: 2, 2022: 4, 2021: 5, 2020: 7Per-year citation counts (last 5 years)
- References (count)
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177Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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