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. 2017 Sep 14;7:11552. doi: 10.1038/s41598-017-11776-y

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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The proposed mechanism of rIAPP aggregation/oligomerization as determined in STZ-induced diabetes in rats. The STZ produced cell stress, increasing protein aggregation and decreasing the capacity for proteostasis. rIAPP undergoes structural perturbations and enters an aggregation-competent state (misfolded), which may even contain β-breakers. The misfolded rIAPP takes on amyloidogenic features, leading to self- and hetero-oligomerization and, finally, conversion into rIAPP fibres. The cytotoxic oligomers cause apoptosis in several cells and the appearance of cross-seeding amyloid structures.