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Synlett 2000; 2000(5): 0575-0586
DOI: 10.1055/s-2000-6590
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Formation of β-Sheet Assemblage with a View to Developing an Amyloid Model

Norihiro Yamada* , Katsuhiko Ariga
  • *Faculty of Education, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263-8522, Japan
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Publication Date:
31 December 2000 (online)

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Amphiphilic molecules that contain a tripeptide moiety form an aggregate not only in water but also in organic solvents. The aggregate possesses fibrous morphology and involves a rich amount of parallel β-sheet structure of peptides, which is similar to a β-amyloid peptide called an amyloid fibril. The dynamic properties of the aggregate of the tripeptide-containing amphiphiles were also similar to those of the amyloid. These similarities suggest that the tripeptide-containing amphiphiles are suitable for an amyloid model.

amyloid - β-sheet structure - organogel - hydrogen bonding - peptide-containing amphiphile

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