Random Heteropolymer Self-Assembly into Protein-Like Nanoparticles

Single-chain polymer nanoparticles are currently of great interest due to their potential applications, yet their properties have only recently started to be elucidated. Here, we study self-assembled single polymer nanoparticles to gain molecular insights into their structure and dynamics using molecular dynamics simulations. In particular, we study a four-component synthetic heteropolymer that has been experimentally investigated previously. Prior experimental findings showed favorable interactions with native proteins in non-native environments and during protein folding. Simulations of single chains demonstrate a rich energy landscape for these polymers, evident from the structure and dynamics of the molecules in solution. Specifically, spatial arrangement of amphiphilic monomers is characterized and shows many parallels to biological proteins. Multiple time scales are seen in system dynamics, showing a large impact of component chemistry and sterics. By bridging the gap between angstrom-scale NMR and bulk characterization, all-atom simulations provide valuable insight into potential mechanisms for these heteropolymer’s behavior.