Compelling evidence strongly suggests that the conversion of a normal soluble protein into a beta-sheet-rich oligomeric structure and further fibril formation is the critical step in the pathogenesis of several human diseases, termed protein misfolding disorders. Therefore, a promising therapeutic strategy consists of the design of molecules that prevent the misfolding and aggregation of these proteins. In this chapter, we survey the mechanism of protein misfolding and some strategies to rationally produce inhibitors of this process.
|Original language||English (US)|
|Number of pages||17|
|Journal||Methods in molecular biology (Clifton, N.J.)|
|State||Published - Jan 1 2006|
ASJC Scopus subject areas
- Molecular Biology