title: Inhibition of protein misfolding and aggregation by small rationally-designed peptides.
abstract: Several human diseases are associated with the presence of toxic fibrillar protein deposits. These diseases called protein misfolding disorders, are characterized by the accumulation of misfolded protein aggregates in diverse tissues. Strong evidence indicates that the conversion of a normal soluble protein into a beta-sheet-rich oligomeric structure and further fibrillar aggregation are the key events in the disease pathogenesis. Therefore, a promising therapeutic target consists of the prevention and dissolution of misfolded protein aggregates. Peptides designed to specifically bind to the pathogenic protein and block and/or reverse its abnormal conformational change constitute a new class of drugs. This article reviews this approach, describing diverse compounds reported to have this activity.
authors.affiliation: Protein Misfolding Disorders Laboratory, George and Cynthia Mitchell Center for Alzheimer's Disease Research, Department of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, USA.
authors.forename: L D
authors.initials: LD
authors.lastname: Estrada
authors.forename: C
authors.initials: C
authors.lastname: Soto
mesh_terms: D015195:Drug Design; D006801:Humans; D019636:Neurodegenerative Diseases / Q000188:drug therapy / Q000235:genetics*; D010455:Peptides / Q000737:chemistry / Q000627:therapeutic use; D017510:Protein Folding
chemical_list: D010455:Peptides