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Biopolymers. 2017 Mar;108(2). doi: 10.1002/bip.22882.

Unraveling the aggregation propensity of human insulin C-peptide.

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Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
Department of Pharmacy, University of Patras, Patras, 26504, Greece.


Over the last 20 years, proinsulin C-peptide emerged as an important player in various biological events. Much time and effort has been spent in exploring all functional features of C-peptide and recording its implications in Diabetes mellitus. Only a few studies, though, have addressed C-peptide oligomerization and link this procedure with Diabetes. The aim of our work was to examine the aggregation propensity of C-peptide, utilizing Transmission Electron Microscopy, Congo Red staining, ATR-FTIR, and X-ray fiber diffraction at a 10 mg ml-1 concentration. Our experimental work clearly shows that C-peptide self-assembles into amyloid-like fibrils and therefore, the aggregation propensity of C-peptide is a characteristic novel feature that should be related to physiological and also pathological conditions.


amyloidogenic peptides; amyloids; diabetes mellitus; insulin biosynthesis; proinsulin C-peptide

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