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PrP charge structure encodes interdomain interactions.

Javier Martínez1, Rosa Sánchez1, Milagros Castellanos2

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Summary
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Protein charge distribution guides structure and function. Cellular prion protein (PrP(C)) charge patterns control its stability, prevent fibrillation, and regulate cleavage, ensuring normal function and reducing disease risk.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Neuroscience

Background:

  • Proteins utilize charged residues for crucial ionic interactions in folding, binding, and catalysis.
  • The cellular prion protein (PrP(C)) possesses a unique two-domain charge distribution impacting its structural flexibility.
  • The precise role of PrP(C) charge distribution in its conformational and metabolic characteristics remains largely unexplored.

Purpose of the Study:

  • To investigate the functional significance of charge distribution within the cellular prion protein (PrP(C)).
  • To elucidate how specific charge patterns influence PrP(C) structure, stability, and fibrillation propensity.
  • To determine the impact of charge interactions on PrP(C) cleavage and fibril formation.

Main Methods:

  • Generation of charge-reverted mutants of PrP(C) domains.
  • Dynamic light scattering and thermal denaturation assays to assess protein structure and stability.
  • Circular dichroism, atomic-force microscopy, and fluorescence microscopy to analyze fibrillar states.

Main Results:

  • Identified electrostatic compensation between the polybasic region (23-30) and the α3 surface compacts the α-fold, enhancing stability and reducing fibrillation.
  • Demonstrated that N-terminal electropositive clusters independently regulate α-cleavage efficiency.
  • Revealed that in fibrillar states, N-terminal positive clusters and the α3 surface dictate secondary structure, assembly, and fibril length.

Conclusions:

  • PrP(C) charge distribution acts as a regulatory code, essential for maintaining normal protein function.
  • Specific charge interactions within PrP(C) are critical for preventing pathogenic misfolding and aggregation.
  • Understanding PrP(C) charge patterns offers insights into prion diseases and potential therapeutic strategies.