Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides.

@article{Rijkers2002InhibitionOA,
  title={Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides.},
  author={Dirk T. S. Rijkers and Jo W. M. H{\"o}ppener and George Posthuma and C. J. Lips and Rob M. J. Liskamp},
  journal={Chemistry},
  year={2002},
  volume={8 18},
  pages={4285-91}
}
Amyloid deposits are formed as a result of uncontrolled aggregation of (poly)peptides or proteins. Today several diseases are known, for example Alzheimer's disease, Creutzfeldt-Jakob disease, mad cow disease, in which amyloid formation is involved. Amyloid fibrils are large aggregates of beta-pleated sheets and here a general method is described to introduce molecular mutations in order to achieve disruption of beta-sheet formation. Eight backbone-modified amylin derivatives, an amyloidogenic… CONTINUE READING

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