Cyclic N-terminal loop of amylin forms non amyloid fibers.

@article{Cope2013CyclicNL,
  title={Cyclic N-terminal loop of amylin forms non amyloid fibers.},
  author={Stephanie M. Cope and Sandip Shinde and Robert B. Best and Giovanna Ghirlanda and Sara M. Vaiana},
  journal={Biophysical journal},
  year={2013},
  volume={105 7},
  pages={
          1661-9
        }
}
We report for the first time, to our knowledge, that the N-terminal loop (N_loop) of amylin (islet amyloid polypeptide (IAPP) residues 1-8) forms extremely long and stable non-β-sheet fibers in solution under the same conditions in which human amylin (hIAPP) forms amyloid fibers. This observation applies to the cyclic, oxidized form of the N_loop but not to the linear, reduced form, which does not form fibers. Our findings indicate a potential role of direct N_loop-N_loop interactions in hIAPP… CONTINUE READING
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References

Publications referenced by this paper.
SHOWING 1-10 OF 61 REFERENCES

Evidence for a partially structured state of the amylin monomer

  • S. M. Vaiana, R. B. Best, J. Hofrichter
  • Biophys. J. 97:2948–2957
  • 2009
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