Journal
BIOPOLYMERS
Volume 108, Issue 2, Pages -Publisher
WILEY
DOI: 10.1002/bip.22882
Keywords
insulin biosynthesis; proinsulin C-peptide; diabetes mellitus; amyloids; amyloidogenic peptides
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Funding
- University of Athens
- European Union (European Regional Development Fund - ERDF)
- General Secretariat for Research and Technology of the Greek Ministry of Education and Religious Affairs, Culture and Sports [11SYN-1-1230]
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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. (C) 2016 Wiley Periodicals, Inc.
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