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

Unraveling the aggregation propensity of human insulin C-peptide.

Author information

1
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
2
Department of Pharmacy, University of Patras, Patras, 26504, Greece.

Abstract

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.

KEYWORDS:

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

PMID:
27257781
DOI:
10.1002/bip.22882
[Indexed for MEDLINE]

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