Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin.

@article{Noormgi2010ZnIIIC,
  title={Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin.},
  author={Andra Noorm{\"a}gi and Julia Gavrilova and J. Smirnova and Vello T{\~o}ugu and Peep Palumaa},
  journal={The Biochemical journal},
  year={2010},
  volume={430 3},
  pages={511-8}
}
Insulin, a 51-residue peptide hormone, is an intrinsically amyloidogenic peptide, forming amyloid fibrils in vitro. In the secretory granules, insulin is densely packed together with Zn(II) into crystals of Zn(2)Insulin(6) hexamer, which assures osmotic stability of vesicles and prevents fibrillation of the peptide. However, after release from the pancreatic beta-cells, insulin dissociates into active monomers, which tend to fibrillize not only at acidic, but also at physiological, pH values… CONTINUE READING

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