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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Peptide amyloid surface display.

Marisa A Rubio1, Diana E Schlamadinger, Ellen M White

  • 1Department of Molecular Biophysics and Biochemistry, Yale University , 260 Whitney Avenue, New Haven, Connecticut 06520-8114, United States.

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Researchers designed a protein scaffold to study amyloid fiber surfaces. This scaffold successfully attenuated islet amyloid polypeptide (IAPP) self-assembly and reduced IAPP-induced toxicity in cells.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Homomeric self-assembly of peptides into amyloid fibers is implicated in numerous diseases.
  • The lateral surface of amyloid fibers is hypothesized to play a key role in toxic gain-of-function mechanisms.

Purpose of the Study:

  • To investigate the role of the lateral fiber surface in amyloid formation and toxicity.
  • To design and utilize a protein scaffold presenting discrete amyloid subdomains.

Main Methods:

  • Designed a protein scaffold to present parallel β-sheet surfaces for amyloid subdomains (up to eight residues).
  • Prepared scaffolds presenting the surface of islet amyloid polypeptide (IAPP).
  • Assessed the effects of these scaffolds on IAPP self-assembly rates in solution and IAPP-induced toxicity in insulin-secreting cells.

Main Results:

  • The designed scaffolds demonstrated sequence-specific surface effects.
  • Scaffolds successfully attenuated the rates of IAPP self-assembly in solution.
  • The scaffolds affected IAPP-induced toxicity in insulin-secreting cells.

Conclusions:

  • The lateral surface of amyloid fibers significantly influences amyloid self-assembly and associated toxicity.
  • Protein scaffolds can be effectively used to probe and modulate amyloidogenic processes.
  • Targeting specific surfaces of amyloid fibers offers a potential therapeutic strategy for amyloid-related diseases.