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