# Effect of Grafting on Aggregation of Intrinsically Disordered Proteins

## TL;DR

This study uses computer simulations to compare how intrinsically disordered proteins aggregate when grafted to a surface versus when free in solution, revealing implications for experimental analysis and aggregation control.

## Contribution

It introduces a modeling approach for IDP aggregation considering grafting effects, providing insights into how surface attachment influences aggregation behavior.

## Key findings

- Grafting alters aggregation propensity of IDPs.
- Grafted IDPs show different aggregation patterns than free IDPs.
- Grafting could be used to suppress harmful aggregation.

## Abstract

A significant part of the proteome is composed of intrinsically-disordered proteins (IDPs). These proteins do not fold into a well-defined structure and behave like ordinary polymers. In this work we consider IDPs which have the tendency to aggregate, model them as heteropolymers that contain a small number of associating monomers and use computer simulations in order to compare the aggregation of such IDPs that are grafted to a surface or free in solution. We then discuss how such grafting may affect the analysis of in-vitro experiments and could also be used to suppress harmful aggregation.