To cite this article:
Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay
Article first published online: 5 DEC 2008
The Journal of Peptide Research
Volume 58, Issue 4, pages 342–346, October 2001
How to Cite
Watanabe, K., Segawa, T., Nakamura, K., Kodaka, M., Okuno, H. and Konakahara, T. (2001), Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay. The Journal of Peptide Research, 58: 342–346. doi: 10.1034/j.1399-3011.2001.00920.x
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.
- Issue published online: 5 DEC 2008
- Article first published online: 5 DEC 2008
- Dates: Received 9 March 2001 Revised 3 May 2001 Accepted 6 July 2001
- Alzheimer's disease;
- β amyloid;
- fluorescence assay;
- molecular interaction;
- molecular probe
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.