. The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation. Sci Adv. 2018 Jun;4(6):eaaq1702. Epub 2018 Jun 29 PubMed.


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  1. For the first time, the authors present compelling evidence that S100B is a direct molecular chaperone for Aβ. The upshot is that, at physiological concentrations and with help from Ca2+, a promiscuous S100B motif binds to Aβ monomers and prevents aggregation.

    At face value, this may seem to contrast with prior work from our group showing that S100B transgenic-mutant human APP/PS1 mice have exacerbated AD-like pathology.  However, as is typical with many protein-protein interactions, binding kinetics are exquisitely concentration-dependent—in this case, stabilizing Aβ monomers at physiological S100B levels but promoting Abβ aggregation at supraphysiological abundance.

    View all comments by Terrence Town

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  1. New Role for Cytokine S100B: Inhibiting Amyloid Aggregation