New Drug Leads For Protein Misfolding | Chemical & Engineering News
Volume 90 Issue 2 | p. 32 | Concentrates
Issue Date: January 9, 2012

New Drug Leads For Protein Misfolding

Screen of some 900,000 molecules turns up compounds that help prevent unwanted protein aggregation
Department: Science & Technology
News Channels: Biological SCENE
Keywords: chaperones, protein folding, proteostasis, protein aggregation, neurodegenerative diseases

A research team led by Northwestern University’s Richard I. Morimoto has discovered new compounds that could become promising leads for drugs to treat Alzheimer’s disease and other protein-misfolding-related conditions (Nat. Chem. Biol., DOI: 10.1038/nchembio.763). Formation of clumps of proteins that are no longer properly folded, a process called aggregation, is a common underlying cause of neurodegenerative and other age-related diseases. Morimoto and coworkers carried out one of the most systematic efforts to date to search for small molecules that could treat such diseases by enhancing proteostasis, a cellular process that promotes protein folding and prevents unwanted protein aggregation. The researchers screened about 900,000 small molecules for compounds that promote proteostasis by increasing cellular production of molecular chaperones—proteins that assist other proteins in folding. The study uncovered seven classes of compounds that boosted chaperone expression and restored protein folding in cell culture and in nematode disease models. Chaperone expert Arthur L. Horwich of Yale University comments that, although it’s a long way from cells and worms to people, it would be wonderful “to find that one could manipulate chaperone expression pharmacologically to benefit misfolding-associated diseases.”

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