SARS-CoV-2 Protein Fragment and Its Effect on Amyloid Formation
Author Information
Author(s): Bilog Marvin, Cersosimo Jennifer, Vigil Iliana, Desamero Ruel Z. B., Profit Adam A.
Primary Institution: City University of New York
Hypothesis
Can a SARS-CoV-2 protein fragment interact with human islet amyloid polypeptide and affect its aggregation?
Conclusion
The SARS-CoV-2 protein fragment SK9 can inhibit the self-assembly of certain amyloidogenic peptides but has little effect on full-length amylin.
Supporting Evidence
- SK9 inhibits the self-assembly of hIAPP12–18 and hIAPP20–29 peptides.
- SK9 has little effect on the aggregation of full-length amylin.
- Docking studies suggest SK9 interacts more strongly with hIAPP12–18 than with hIAPP20–29.
Takeaway
A piece of a virus can stop some proteins in our body from sticking together and forming harmful clumps, but it doesn't work on the full protein.
Methodology
The study used molecular dynamics simulations, docking studies, and biophysical techniques to investigate interactions between SK9 and hIAPP peptides.
Limitations
The study did not find significant effects of SK9 on the aggregation of full-length amylin, which contradicts some previous simulations.
Digital Object Identifier (DOI)
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