Fig. 2.

DMD simulations of βCas binding with AuNP, Aβ monomer, and oligomer. a Binding probabilities of βCas with an AuNP, an Aβ monomer and an Aβ oligomer, where high-binding is defined as residues with binding probabilities above one standard deviation from the average (dash lines). βCas high-binding residue regions with AuNP and with Aβ monomer/oligomer are highlighted with bars (inset). b Predicted CD spectra of secondary structure contents (inset) derived from simulations. c Predicted βCas-AuNP corona structures comprised of three βCas proteins on an AuNP surface (right) and corresponding molecular surfaces of the proteins (left) are shown to highlight their binding with an Aβ monomer, where each βCas residue was colored from purple (low) to red (high) according to its binding probability with Aβ monomer as in panel A middle. Source data are provided as a Source Data file