Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay

Authors


  • To cite this article:

    Watanabe, K-i., Segawa, T., Nakamura, K., Kodaka, M., Konakahara, T. & Okuno, H. Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay.

    J. Peptide Res., 2001, 58, 342–346.

Kazuhiko Nakamura
National Institute of Advanced Industrial Science and Technology (AIST)
Central 6
1-1 Higashi
Tsukuba
Ibaraki 305-8566
Japan
Tel.: 81-298-61-6186
Fax: 81-298-61-6123
E-mail: kazuhiko.nakamura@aist.go.jp

Abstract

Abstract: β-Amyloid peptides (Aβ) are the main protein components of neuritic plaques and are important in the pathogenesis of Alzheimer's disease. It is reported that Aβ 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 Aβ aggregate. A specific interaction was observed between labeled and immobilized KLVFF. It suggests that the aggregation of Aβ was controlled by the recognition of KLVFF itself by hydrophobic and electrostatic interactions.

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