title: Unraveling the aggregation propensity of human insulin C-peptide.
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-1concentration. 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.
authors.affiliation: Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
authors.forename: Paraskevi L
authors.initials: PL
authors.lastname: Tsiolaki
authors.affiliation: Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
authors.forename: Nikolaos N
authors.initials: NN
authors.lastname: Louros
authors.affiliation: Department of Pharmacy, University of Patras, Patras, 26504, Greece.
authors.forename: Aikaterini A
authors.initials: AA
authors.lastname: Zompra
authors.affiliation: Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
authors.forename: Stavros J
authors.initials: SJ
authors.lastname: Hamodrakas
authors.affiliation: Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Panepistimiopolis, Athens, 15701, Greece.
authors.forename: Vassiliki A
authors.initials: VA
authors.lastname: Iconomidou
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D002096:C-Peptide / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D003224:Congo Red / Q000737:chemistry; D003920:Diabetes Mellitus / Q000378:metabolism; D006801:Humans; D007328:Insulin / Q000737:chemistry* / Q000378:metabolism; D046529:Microscopy, Electron, Transmission; D008859:Microscopy, Polarization; D018715:Microscopy, Video; D066263:Protein Aggregation, Pathological; D011487:Protein Conformation; D055503:Protein Multimerization; D017550:Spectroscopy, Fourier Transform Infrared; D013194:Staining and Labeling / Q000379:methods; D014961:X-Ray Diffraction
chemical_list: D000682:Amyloid; D002096:C-Peptide; D007328:Insulin; D003224:Congo Red
keywords: amyloidogenic peptides; amyloids; diabetes mellitus; insulin biosynthesis; proinsulin C-peptide