Mechanism of thioflavin T binding to amyloid fibrils

  • Apostol M
  • Wiltzius J
  • Sawaya M
 et al. 
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Abstract

The amylome is the universe of proteins that are capable of forming amyloid-like fibrils. Here we investigate the factors that enable a protein to belong to the amylome. A major factor is the presence in the protein of a segment that can form a tightly complementary interface with an identical segment, which permits the formation of a steric zipper-two self-complementary beta sheets that form the spine of an amyloid fibril. Another factor is sufficient conformational freedom of the self-complementary segment to interact with other molecules. Using RNase A as a model system, we validate our fibrillogenic predictions by the 3D profile method based on the crystal structure of NNQQNY and demonstrate that a specific residue order is required for fiber formation. Our genome-wide analysis revealed that self-complementary segments are found in almost all proteins, yet not all proteins form amyloids. The implication is that chaperoning effects have evolved to constrain self-complementary segments from interaction with each other.

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  • 03
  • 03856
  • 31st European Peptide Symposium
  • 3D domain swapping
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  • ??-Amylase
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  • Amyloid beta-Protein Precursor
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  • Thioflavin T
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  • α -helix
  • β -helix
  • β-sheet helix

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Authors

  • Marcin I. Apostol

  • Jed J. W. Wiltzius

  • Michael R. Sawaya

  • Duilio Cascio

  • David S Eisenberg

  • Melinda Balbirnie

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