A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide
Castelletto, V., Hamley, I. W., Lim, T., De Tullio, M. B. and Castaño, E. M. (2010) A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide. Journal of Peptide Science, 16 (9). pp. 443-450. ISSN 1099-1387
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To link to this article DOI: 10.1002/psc.1271
We study the complex formation of a peptide betaAbetaAKLVFF, previously developed by our group, with Abeta(1–42) in aqueous solution. Circular dichroism spectroscopy is used to probe the interactions between betaAbetaAKLVFF and Abeta(1–42), and to study the secondary structure of the species in solution. Thioflavin T fluorescence spectroscopy shows that the population of fibers is higher in betaAbetaAKLVFF/Abeta(1–42) mixtures compared to pure Abeta(1–42) solutions. TEM and cryo-TEM demonstrate that co-incubation of betaAbetaAKLVFF with Abeta(1–42) causes the formation of extended dense networks of branched fibrils, very different from the straight fibrils observed for Abeta(1–42) alone. Neurotoxicity assays show that although betaAbetaAKLVFF alters the fibrillization of Abeta(1–42), it does not decrease the neurotoxicity, which suggests that toxic oligomeric Abeta(1–42) species are still present in the betaAbetaAKLVFF/Abeta(1–42) mixtures. Our results show that our designed peptide binds to Abeta(1–42) and changes the amyloid fibril morphology. This is shown to not necessarily translate into reduced toxicity.
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