|
|
|
| |
 |
|
| |
January 13,
2005
|
|
|
|
|
| |
More ammo for Huntington's disease arsenal
Compound that inhibits protein aggregation could lead to therapeutics |
|
|
|
|
|
SOPHIE L. ROVNER
|
|
| |
|
|
| |
Huntington’s disease is caused by a mutation in the gene that codes for huntingtin. Mutated huntingtin contains extra polyglutamine (polyQ), an alteration that causes the protein to misfold and aggregate into clumps. Researchers haven’t yet settled whether the neurodegeneration that results from the disease is caused by these huntingtin aggregates, by the toxicity of smaller precursors, or by some other mechanism.
Aleksey G. Kazantsev of Massachusetts General Hospital, in Charlestown, and colleagues have now come up with evidence that they believe supports the aggregate hypothesis [Proc. Natl. Acad. Sci. USA, 102, 892 (2005)]. The researchers used a high-throughput screening assay to find molecules that inhibit polyQ-dependent aggregation in yeast. They then tested structural analogs of the most potent inhibitors.
The most effective compound they found (shown) significantly reduces neurodegeneration in a Drosophila model of Huntington’s. This compound and three others “are strong lead compounds for the development of therapeutics” for the disease, the team notes.
|
|
| |
|
|
| |
Chemical & Engineering News
ISSN 0009-2347
Copyright © 2004 |
|
|
|
|
