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. 2013 Nov 18;288(52):37104–37111. doi: 10.1074/jbc.M113.513432

FIGURE 1.

FIGURE 1.

ZAβ3W as a probe for Aβ protofibril dissociation. A, model of the ZAβ3W-Aβ complex. Tyr-18 in both subunits (blue and marine) of ZAβ3 (Protein Data Bank entry 2OTK) was replaced by tryptophan (red sticks). Aβ(16–40) is shown in orange. B, scheme of protofibril dissociation monitored by binding of Aβ monomers to ZAβ3W. C, fluorescence emission spectra of ZAβ3W in the absence (red) and presence (blue) of a stoichiometric amount of Aβ42 monomers and spectra of free Aβ42 (magenta) and buffer (black). D, λmax of fluorescence emission spectra of simulated mixtures of free and bound ZAβ3W (●). The line represents a fit to an exponential function employed to calculate the fraction of free ZAβ3W from experimentally determined λmax values.