Unraveling the Aggregation Propensity of Human Insulin C-Peptide

作者：Tsiolaki Paraskevi L; Louros Nikolaos N; Zompra Aikaterini A; Hamodrakas Stavros J; Iconomidou Vassiliki A^*

来源：Biopolymers, 2017, 108(2): 22882.

DOI：10.1002/bip.22882

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

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.

• 出版日期2017-3