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Cholesterol Secosterol Adduction Inhibits the Misfolding of a Mutant Prion Protein Fragment that Induces Neurodegeneration
Author(s) -
Scheinost Johanna C.,
Witter Daniel P.,
Boldt Grant E.,
Offer John,
Wentworth Paul
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904524
Subject(s) - fragment (logic) , neurodegeneration , prion protein , protein folding , computational biology , chemistry , mechanism (biology) , aldehyde , biochemistry , medicine , biology , computer science , disease , philosophy , programming language , catalysis , epistemology
Aldehyde is critical: Atheronal‐B, a cholesterol secosterol aldehyde (see structure), completely inhibits the misfolding of a prion protein fragment from its α to β form through a mechanism that involves adduction to the protein. This result offers a fresh view of lipid aldehyde‐induced protein misfolding and provides a promising molecular scaffold on which to develop potential prion disease therapeutics.

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