The effect of tachykinin neuropeptides on amyloid β aggregation

Efrat Flashner, Uri Raviv*, Assaf Friedler

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


A hallmark of Alzheimer's disease is production of amyloid β peptides resulting from aberrant cleavage of the amyloid precursor protein. Amyloid β assembles into fibrils under physiological conditions, through formation of neurotoxic intermediate oligomers. Tachykinin peptides are known to affect amyloid β neurotoxicity in cells. To understand the mechanism of this effect, we studied how tachykinins affect Aβ(1-40) aggregation in vitro. Fibrils grown in the presence of tachykinins exhibited reduced thioflavin T (ThT) fluorescence, while their morphology, observed in transmission electron microscopy (TEM), did not alter. Cross linking studies revealed that the distribution of low molecular weight species was not affected by tachykinins. Our results suggest that there may be a specific interaction between tachykinins and Aβ(1-40) that allows them to co-assemble. This effect may explain the reduction of Aβ(1-40) neurotoxicity in cells treated with tachykinins.

Original languageAmerican English
Pages (from-to)13-17
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 1 Apr 2011

Bibliographical note

Funding Information:
AF is supported by a starting grant from the European Research Council under the European Community’s Seventh Framework Programme (FP7/2007-2013)/ERC Grant agreement No: 203413. UR is supported by the US–Israel Bi-national Science Foundation (Grant number 2005-234), The Human Frontier Science Program Organization (Career Development Award, CDA 0059/2006), the James Frank program, Safra, Wolfson and Rudin foundations. We thank Tim Deming, Hermona Soreq, Erez Podoly, Alik Belitzky, Sophia Diamant, Inna Solomonov, Chaim Gilon and Daniel Harries for helpful discussions.


  • Aggregation
  • Amyloid β
  • Co-assembly
  • Neuropeptides
  • Self-assembly
  • Tachykinins


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