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January 25, 2026

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Structural Basis of Glycoform Selectivity in Prion Strains

FPFrancesca PeccatiIkerbasque

Key Points

To elucidate the structural mechanisms underlying glycoform selectivity in prion strains.
Analyzed the conformational differences of PrP C and PrP Sc
Examined the aggregation propensity of various glycoforms
Utilized structural biology techniques to assess conformational stability
Identified distinct structural features that influence glycoform selectivity
Showed varying aggregation rates corresponding to glycoform variations
Revealed insights into the relationship between glycoform structure and pathogenicity

Abstract

Prion diseases originate from the pathological misfolding of the cellular sialoglycoprotein prion protein (PrP C ), universally found across mammalian species, into an aberrant conformation termed PrP Sc , which exhibits high aggregation propensity...

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Cite This Study

Francesca Peccati (Thu,) studied this question.

synapsesocial.com/papers/6975b1eafeba4585c2d6d6a5 https://doi.org/https://doi.org/10.1039/d5cp04286k

Structural Basis of Glycoform Selectivity in Prion Strains | Synapse