Extended Data Fig. 6: The BRICHOS domain inhibits secondary nucleation of Aβ42 aggregation and the membrane disruption ability of Aβ42 oligomers. | Nature Structural & Molecular Biology

Extended Data Fig. 6: The BRICHOS domain inhibits secondary nucleation of Aβ42 aggregation and the membrane disruption ability of Aβ42 oligomers.

From: Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation

Extended Data Fig. 6

a, Monomeric Aβ42 was incubated at a concentration of 2 μM in the presence of 20 μM ThT at 37 °C under quiescent conditions in the absence (black) and presence (dark blue: 10%, cyan: 35%, magenta: 50%, green: 75% and orange 100% relative to monomeric Aβ42) of the Brichos domain. b, Fits to the kinetic traces of the aggregation reactions in the presence of the BRICHOS domain to determine its influence on secondary nucleation. c, Relative secondary nucleation rate constants k2 of the aggregation of Aβ42 with increasing concentrations of the BRICHOS domain. d, Drawing of the microscopic events of Aβ42 aggregation in the presence of the BRICHOS domain that inhibits secondary nucleation.

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