Exploiting Cross-Amyloid Interactions To Inhibit Protein Aggregation but not Function: Nanomolar Affinity Inhibition of Insulin Aggregation by an IAPP Mimic


  • We are grateful to S. Stevanovic and C. Henkel for MALDI measurements, J. Bernhagen for help in establishing the insulin receptor assays, and L. M. Yan for helpful discussions and preliminary studies on insulin fibrillization. This work was supported by the Deutsche Forschungsgemeinschaft (DFG).


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Potential aggregate preventer: The designed peptide IAPP-GI inhibits the non-native aggregation of insulin without affecting its function. As the peptide also blocks aggregation of key amyloid peptides that occur in Alzheimer's disease and type II diabetes, it is a promising drug candidate.