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Search for New Aggregable Fragments of Human Insulin

Institute of Organic Chemistry, Lodz University of Technology, Zeromskiego 116, 90-924 Lodz, Poland
Institute of Mechatronics and Information Systems, Faculty of Electrical, Electronic, Computer and Control Engineering, Lodz University of Technology, Stefanowskiego 18/22, 90-924 Lodz, Poland
Author to whom correspondence should be addressed.
Molecules 2019, 24(8), 1600;
Received: 18 March 2019 / Revised: 18 April 2019 / Accepted: 20 April 2019 / Published: 23 April 2019
PDF [6152 KB, uploaded 23 April 2019]


In this study, three independent methods were used to identify short fragment of both chains of human insulin which are prone for aggregation. In addition, circular dichroism (CD) research was conducted to understand the progress of aggregation over time. The insulin fragments (deca- and pepta-peptides) were obtained by solid-phase synthesis using 4-(4,6-dimethoxy-1,3,5-triazin-2-yl)-4-methylmorpholinium toluene-4-sulfonate (DMT/NMM/TosO-) as a coupling reagent. Systematic studies allowed identification of the new fragments, expected to be engaged in triggering aggregation of the entire structure of human insulin under physiological conditions. It was found that the aggregation process occurs through various structural conformers and may favor the formation of a fibrous structure of aggregate. View Full-Text
Keywords: Aggregation; amyloid deposits; amyloid-like fiber formation; diabetes; SPPS; triazine coupling reagents Aggregation; amyloid deposits; amyloid-like fiber formation; diabetes; SPPS; triazine coupling reagents

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Swiontek, M.; Fraczyk, J.; Wasko, J.; Chaberska, A.; Pietrzak, L.; Kaminski, Z.J.; Szymanski, L.; Wiak, S.; Kolesinska, B. Search for New Aggregable Fragments of Human Insulin. Molecules 2019, 24, 1600.

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