Fig. 4: Thermodynamic profiling of cross-interactions for the VQIVYK amyloid core. | Nature Communications

Fig. 4: Thermodynamic profiling of cross-interactions for the VQIVYK amyloid core.

From: Mapping the sequence specificity of heterotypic amyloid interactions enables the identification of aggregation modifiers

Fig. 4

a Schematic representation and positioning of the VQIVYK APR in full-length tau. b Quadrant plot analysis of the four modes of interactions for single variants of the VQIVYK APR. c Heterotypic aggregation is promoted by hydrophobic mutations that stabilise the aggregation core, electrostatic interactions that improve surface solubility or improved stacking interactions at the exposed fibril surface. d Capping interactions are facilitated by the incorporation of bulky aromatic residues that blocked further elongation at the fibril tips through steric clashes or charged side chains that blocked elongation through electrostatic repulsion of stacked charges.

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