Premium
A comparative analysis between PrP Sc and α‐synuclein to explore the structure‐function relationships of pathogenic protein misfolding in prion diseases and Parkinson’s disease
Author(s) -
Peterson Alison,
Abdulwali Ahlaam,
Bunday Priscilla,
Fiedor Lauren,
Lee Seyoung,
Merlin Daniela Hernandez,
Morgan Elizabeth,
Torelli Julianna,
Yeoh Ming Ying
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.02807
Subject(s) - alpha synuclein , parkinson's disease , disease , synuclein , protein folding , amyloid (mycology) , prion protein , neurodegeneration , protein aggregation , lewy body , dementia with lewy bodies , biology , neuroscience , medicine , dementia , microbiology and biotechnology , pathology
Prion diseases, or transmissible spongiform encephalopathies (TSEs), are fatal neurodegenerative diseases affecting humans and other mammals, caused when the alpha‐helix rich prion protein (PrP C ) misfolds and converts into a beta‐sheet rich insoluble conformer (PrP Sc ), which aggregates into toxic amyloid structures. The toxic protein misfolding spreads through a “prion‐only” mechanism in which the diseased PrP Sc promotes the misfolding of PrP C . Parkinson’s disease is a neurodegenerative disease characterized by intraneuronal misfolded‐protein aggregates (Lewy bodies and Lewy neurites). Recent research suggests that α‐synuclein may contribute to the pathology of Parkinson’s disease in a prion‐like fashion when a misfolded version of α‐synuclein acts as a template for the misfolding of healthy α‐synuclein, resulting in pathological aggregation. Both prion diseases and Parkinson’s disease cannot be cured and are ultimately fatal. Further exploring the structure‐function relationships in these proteins and how they drive the pathologies of prion diseases and Parkinson’s disease will better our understanding of these diseases. The Minnetonka MSOE Center for BioMolecular Modeling SMART Team used 3D modeling and printing technology to examine the structural similarities and differences of α‐synuclein and the prion protein to further elucidate the mechanisms of pathological protein misfolding.