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We present a generic model to describe the fractal self-assembly of proteinsin terms of electrostatic and hydrophobic interactions. The predictions of themodel were correlated with the simulated fractals obtained using patchydiffusion-limited aggregation, and the experimentally observed Amyloid-\b{eta}(A\b{eta}) fractal self-assembly using confocal microscopy. The moleculardocking was used to determine the properties of the patches on A\b{eta}oligomers. Similar patch properties were used to design the particles forsimulation. In agreement with the model predictions, the free energy offormation for the simulated fractal self-assembly was proportional to itsfractal dimension; moreover, their morphologies were similar to the fractalmorphologies of A\b{eta} observed experimentally at different pH.

Electrostatic and hydrophobic patches on Amyloid-\b{eta} oligomers govern their fractal self-assembly: Implication to proteins