Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis.

@article{Yan2006DesignOA,
  title={Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis.},
  author={Li-Mei Yan and Marianna Tatarek-Nossol and Aleksandra Velkova and Athanasios Kazantzis and Aphrodite Kapurniotu},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 7},
  pages={2046-51}
}
Protein aggregation into cytotoxic oligomers and fibrils in vivo is linked to cell degeneration and the pathogenesis of >25 uncurable diseases, whereas the high aggregation propensity and insolubility of several bioactive polypeptides and proteins in vitro prevent their therapeutic use. Aggregation of human islet amyloid polypeptide (IAPP) into pancreatic amyloid is strongly associated with the pathogenesis of type II diabetes. IAPP is a 37-residue polypeptide that acts as a neuroendocrine… CONTINUE READING

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Methods in Enzymology: Amyloid, Prions, and Other Protein Aggregates, ed

  • H. LeVine
  • San Diego),
  • 1999
1 Excerpt

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