title: Protein misfolding disorders and rational design of antimisfolding agents.
abstract: 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.
authors.affiliation: Protein Misfolding Disorders Laboratory, Department of Neurology, University of Texas Medical Branch, Galveston, TX, USA.
authors.forename: Lisbell D
authors.initials: LD
authors.lastname: Estrada
authors.forename: June
authors.initials: J
authors.lastname: Yowtak
authors.forename: Claudio
authors.initials: C
authors.lastname: Soto
mesh_terms: D000682:Amyloid / Q000037:antagonists & inhibitors; D000818:Animals; D015195:Drug Design; D030342:Genetic Diseases, Inborn / Q000188:drug therapy* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000627:therapeutic use; D011489:Protein Denaturation / Q000187:drug effects; D015202:Protein Engineering / Q000379:methods; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D000682:Amyloid; D010455:Peptides