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

TL;DR

This study introduces a generic model linking electrostatic and hydrophobic interactions to the fractal self-assembly of proteins, validated through simulations and experimental observations of Amyloid-eta oligomers.

Contribution

The paper presents a novel model that predicts protein fractal assembly based on patch properties, validated by simulations and experimental data.

Findings

Model predicts free energy proportional to fractal dimension.

Simulated and experimental fractals show similar morphologies.

Patch properties determine assembly behavior.

Abstract

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