Abstract

Prion protein (PrP) has two regions: unstructured region PrP(1-120) and structured region PrP(119-231). In the structured region, there are many segments which have the property of amyloid fibril formation. By theoretical calculations, PrP(126-133), PrP(137-143), PrP(170-175), PrP(177-182), PrP(211-216) have the amyloid fibril forming property. PrP(142-166) has a X-ray crystallography experimental β-hairpin structure, instead of a pure cross-β amyloid fibril structure; thus we cannot clearly find it by our theoretical calculations. However, we can predict that there must be a laboratory X-ray crystal structure in PrP(184-192) segment that will be produced in the near future. The experiments of X-ray crystallography laboratories are agreeing with our theoretical calculations. This article summarized mathematical formulas of prion amyloid fibril cross-β structures of all the above PrP segments currently listed in the Protein Data Bank.

Highlights

  • Prion protein (PrP) has two regions: unstructured region PrP(1-120) and structured region PrP(119-231)

  • 10.Figure 10, mathematical formulas for CD, EF, GH Chains obtained from the basic AB Chains respectively are

  • All the above X-ray crystallography structures show to us, in the PrP(119-231) structured region, there are many segments of peptides which can formulate into amyloid fibrils

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Summary

Introduction

Prion protein (PrP) has two regions: unstructured region PrP(1-120) and structured region PrP(119-231). 1. Figure 1, the mathematical formula for B Chain got from A Chain is PDB ID Class of the cross-β 3. Figure 3, mathematical formulas for CD, EF, GH, IJ, KL Chains obtained from AB Chains respectively are

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