FIGURE

Figure 2

ID

ZDB-FIG-201003-60

Publication

Javed et al., 2020 - Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC

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Figure 2

DMD simulations of molecular interactions between FapC and Aβ. A) The averaged binding frequency of each FapC with Aβ42 monomer (top) and the corresponding β‐sheet structure propensity (bottom). The results were obtained from binding simulations of Aβ42 with 10‐residue FapC with overlapping sequences. B) Mass‐weighted average cluster or aggregate sizes (top left) and β‐sheet contents (top right) obtained from aggregation simulations of six tested peptides, including three Aβ‐binding hotspot fragments and three controls for comparison. Typical snapshots of these cases formed β‐sheet rich aggregates (bottom). FapC was individually colored. C) Overlaying of final snapshots from ten independent cross‐seeding simulations, where preformed nanofibril by FapC41‐50 was shown as cartoon with molecular surface colored according to each residue's binding probability with Aβ from low (blue) to high (red). Aβ42 atoms were shown in wheat spheres. D) The intermolecular center‐of‐mass (COM) distance distribution between Aβ42 and the FapC nanofibril. Representative structures as cartoon were shown for each peak as inset with FapCS colored in gray and Aβ42 in rainbow.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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