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A Small‐Molecule Inhibitor of Prion Replication and Mutant Prion Protein Toxicity
Author(s) -
Massignan Tania,
Sangiovanni Valeria,
Biggi Silvia,
Stincardini Claudia,
Elezgarai Saioa R.,
Maietta Giulia,
Andreev Ivan A.,
Ratmanova Nina K.,
Belov Dmitry S.,
Lukyanenko Evgeny R.,
Belov Grigory M.,
Barreca Maria Letizia,
Altieri Andrea,
Kurkin Alexander V.,
Biasini Emiliano
Publication year - 2017
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201700302
Subject(s) - prion protein , mutant , gene isoform , small molecule , toxicity , biology , fungal prion , microbiology and biotechnology , chemistry , biochemistry , gene , phenotype , medicine , disease , organic chemistry , pathology
Into the fold : Prion diseases are neurodegenerative disorders characterized by the accumulation in the brain of a self‐replicating, misfolded isoform (PrP Sc ) of the cellular prion protein (PrP C ). No therapies are available for these pathologies. We capitalized on previously described cell‐based assays to screen a library of small molecules, and identified 55 , a compound capable of counteracting both prion replication and toxicity. Compound 55 may represent the starting point for the development of a completely new class of therapeutics for prion diseases.