Inhibition of Islet Amyloid Polypeptide Fibrillation by Structurally Diverse Phenolic Compounds and Fibril Disaggregation Potential of Rutin and Quercetin
Author:
Affiliation:
1. Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada
2. School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa K1H 8M5, Canada
Funder
University of Ottawa
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.1c06918
Reference48 articles.
1. Potential of peptides and phytochemicals in attenuating different phases of islet amyloid polypeptide fibrillation for type 2 diabetes management
2. Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes
3. Evidence of Cosecretion of Islet Amyloid Polypeptide and Insulin by β-Cells
4. The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet β cells
5. Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus
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3. An investigation into the potential action of polyphenols against human Islet Amyloid Polypeptide aggregation in type 2 diabetes;International Journal of Biological Macromolecules;2023-01
4. Charge modifications of graphene oxide enhance the inhibitory effect on insulin amyloid fibrillation based on electrostatic interactions;International Journal of Biological Macromolecules;2023-01
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