Institute of Organic Chemistry Faculty of Chemistry Lodz University of Technology Zeromskiego 116 Lodz 90-924 Poland
Institute of Applied Computer Science Lodz University of Technology Stefanowskiego Łódź, 18/22 Lodz 90-537 Poland
Institute of General Food Chemistry Faculty of Biotechnology and Food Sciences Lodz University of Technology Stefanowskiego 4/10 Lodz 90-924 Poland
Hirszfeld Institute of Immunology and Experimental Therapy Polish Academy of Sciences 12 Rudolfa Weigla St. 53-114 Wroclaw Poland
Front Cover. Amylin (islet amyloid polypeptide (IAPP)) is one of the hormones that regulate carbohydrate metabolism. Unfortunately, it aggregates, and amyloid aggregates bind to intra‐ and extracellular proteins and proteoglycans to form amyloid deposits which, filling the intercellular space, destroy the normal structure and functions of tissues. Aggregation of IAPP is responsible for extracellular amyloid formation which may contribute to B cells degeneration and impaired insulin secretion. Thinking about the process of inhibition of the aggregation of amylin, it is necessary to disturb the ability of β‐structures to interaction, which translates into inhibition of the deposit growth. Within the aggregating proteins/polypeptides there are hot spots determining the aggregation of the whole protein. Therefore, the search for inhibitors of the aggregation of the proteins/polypeptides is necessary to characterize them. The identified new amylin fragments prone to aggregation may be the starting point for the search for their analogues capable of interacting with the hormone and inhibiting its aggregation ability as reported by Kolesinska et al. in their full paper at10.1002/cbdv.202000501.
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