Cholesterol Secosterol Adduction Inhibits the Misfolding of a Mutant Prion Protein Fragment that Induces Neurodegeneration | Zendy

Scheinost Johanna C. | Zendy; Witter Daniel P. | Zendy; Boldt Grant E. | Zendy; Offer John | Zendy; Wentworth Paul | Zendy

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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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