Small molecule inhibitors of lysozyme amyloid aggregation.
Cell Biochem Biophys
; 44(3): 549-53, 2006.
Article
em En
| MEDLINE
| ID: mdl-16679543
Protein amyloid aggregation is associated with a number of important human pathologies, but the precise mechanisms underlying the toxicity of amyloid aggregates are still incompletely understood. In this context, drugs capable of blocking or interfering with the aggregation of amyloidogenic proteins should be considered in strategies aimed at the development of novel therapeutic agents. Human lysozyme variants have been shown to form massive amyloid deposits in the livers and kidneys of individuals affected by hereditary systemic amyloidosis. Currently, there are no clinical treatments available to prevent or reverse formation of such amyloid deposits. We have recently described a number of di- and trisubstituted aromatic compounds that block the formation of soluble oligomers and amyloid fibrils of the beta-amyloid peptide (Abeta) and protect hippocampal neurons in culture from Abeta-induced toxicity. Here, we show that some of those compounds inhibit the formation and disrupt preformed amyloid fibrils from both human and hen egg white lysozyme. These results suggest that these small molecule compounds may serve as prototypes for the development of drugs for the prevention or treatment of different types of amyloidoses.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Muramidase
/
Peptídeos beta-Amiloides
/
Aminofenóis
/
Amiloide
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Revista:
Cell Biochem Biophys
Assunto da revista:
BIOFISICA
/
BIOQUIMICA
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Estados Unidos