Publication: Methylations of Tryptophan-Modified Naphthoquinone affect its inhibitory potential toward Aβ aggregation
Methylations of Tryptophan-Modified Naphthoquinone affect its inhibitory potential toward Aβ aggregation
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Scherzer-Attali, R., Convertino, M., Pellarin, R., Gazit, E., Segal, D., & Caflisch, A. (2013). Methylations of Tryptophan-Modified Naphthoquinone affect its inhibitory potential toward Aβ aggregation. Journal of Physical Chemistry B, 117(6), 1780–1789. https://doi.org/10.1021/jp309066p
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Aggregation of amyloid beta (Aβ) is the hallmark of Alzheimer's disease (AD). Small molecules inhibiting Aβ can be valuable therapeutics for AD. We have previously reported that 1,4-naphthoquinon-2-yl-l-tryptophan (NQTrp), reduces aggregation and oligomerization of Aβ in vitro and in vivo. In silico analysis further showed that certain functional groups of NQTrp, not in the aromatic rings, are also involved in binding and inhibiting Aβ. To better understand the exact mode of action and identify the groups crucial for NQTrp inhibitory
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- Scherzer-Attali, Roni
- Convertino, Marino
- Pellarin, Riccardo
- Gazit, Ehud
- Segal, Daniel
- Caflisch, Amedeo
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Scherzer-Attali, R., Convertino, M., Pellarin, R., Gazit, E., Segal, D., & Caflisch, A. (2013). Methylations of Tryptophan-Modified Naphthoquinone affect its inhibitory potential toward Aβ aggregation. Journal of Physical Chemistry B, 117(6), 1780–1789. https://doi.org/10.1021/jp309066p
