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Unraveling the aggregation propensity of human insulin C‐peptide
Author(s) -
Tsiolaki Paraskevi L.,
Louros Nikolaos N.,
Zompra Aikaterini A.,
Hamodrakas Stavros J.,
Iconomidou Vassiliki A.
Publication year - 2017
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22882
Subject(s) - peptide , chemistry , proinsulin , c peptide , fibril , amyloid (mycology) , fiber diffraction , biophysics , insulin , biochemistry , medicine , diffraction , biology , x ray crystallography , inorganic chemistry , physics , optics
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. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 108: 1–8, 2017.