Effect of surface chemistry on islet amyloid polypeptide conformation Article Swipe
The formation of dense, linear arrays (fibrils) by biomolecules is the hallmark of a number of degenerative diseases, such as Alzheimer’s and type-2 diabetes. Protein fibrils have also attracted interest as building blocks for new materials. It has long been recognized that surfaces can affect the fibrillation process. Recent work on the model fibril forming protein human islet amyloid polypeptide (hIAPP) has shown that while the protein concentration is highest at hydrophobic surfaces, the rate of fibril formation is lower than on other surfaces. To understand this, replica exchange molecular dynamics simulations were used to investigate the conformations that hIAPP adopts on surfaces of different hydrophobicities. The hydrophobic surface stabilizes α-helical structures which are significantly different to those found on the hydrophilic surface and in bulk solution. There is also a greatly reduced conformational ensemble on the hydrophobic surface due to long-lived contacts between hydrophobic residues on the protein and the surface. This new microscopic information will help us determine the mechanism of the enhancement of fibril formation on surfaces and provides new insight into the effect of nanointerfaces and protein conformation.
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Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1116/6.0000417
- https://avs.scitation.org/doi/pdf/10.1116/6.0000417
- OA Status
- hybrid
- Cited By
- 9
- References
- 67
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3083647847
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
-
https://openalex.org/W3083647847Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1116/6.0000417Digital Object Identifier
- Title
-
Effect of surface chemistry on islet amyloid polypeptide conformationWork title
- Type
-
articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2020Year of publication
- Publication date
-
2020-09-01Full publication date if available
- Authors
-
David L. CheungList of authors in order
- Landing page
-
https://doi.org/10.1116/6.0000417Publisher landing page
- PDF URL
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https://avs.scitation.org/doi/pdf/10.1116/6.0000417Direct link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
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hybridOpen access status per OpenAlex
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https://avs.scitation.org/doi/pdf/10.1116/6.0000417Direct OA link when available
- Concepts
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Fibril, Chemistry, Biomolecule, Biophysics, Amyloid (mycology), Amyloid fibril, Molecular dynamics, Hydrophobic effect, Crystallography, Amyloid β, Biochemistry, Computational chemistry, Pathology, Biology, Disease, Medicine, Inorganic chemistryTop concepts (fields/topics) attached by OpenAlex
- Cited by
-
9Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 1, 2024: 1, 2023: 1, 2022: 2, 2021: 2Per-year citation counts (last 5 years)
- References (count)
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67Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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