Identification of the molecular interaction site of amyloid beta peptide by using a fluorescence assay.
J Pept Res
; 58(4): 342-6, 2001 Oct.
Article
em En
| MEDLINE
| ID: mdl-11606220
ABSTRACT
Beta-amyloid peptides (Abeta) are the main protein components of neuritic plaques and are important in the pathogenesis of Alzheimer's disease. It is reported that Abeta itself is not toxic; however, it becomes toxic to neuronal cells once it has aggregated into amyloid fibrils by peptide-peptide interactions. In this study, to specify the molecular mechanism of aggregation, a novel fluorescence assay was designed. For this purpose, possible partial peptides (38 types of 5-mer) were synthesized on solid-phase. The molecular interactions were examined by a fluorescence probe possessing Lys-Leu-Val-Phe-Phe (KLVFF) as a molecular recognition site. KLVFF is known to be a minimum sequence for formation of the Abeta aggregate. A specific interaction was observed between labeled and immobilized KLVFF. It suggests that the aggregation of Abeta was controlled by the recognition of KLVFF itself by hydrophobic and electrostatic interactions.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
/
Peptídeos beta-Amiloides
/
Doença de Alzheimer
/
Corantes Fluorescentes
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Revista:
J Pept Res
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2001
Tipo de documento:
Article
País de afiliação:
Japão