(362c) Dynamic Behavior of Protein-Inspired Heteropolymers

Amphiphilic synthetic random heteropolymers can provide a bio-inspired means for augmenting and even mimicking bio-macromolecular function. The statistical distribution of chains makes analysis of particular molecules and motifs challenging experimentally. Through atomistic molecular dynamics simulations, we provide nanoscale analysis of individual sequences to provide insight into how these synthetic polymers respond to their environments. Having previously shown multiple dynamic modes and heterogeneous surfaces for the chains in aqueous solution, we now characterize their statistically derived properties in more complex environments. Polymer remodeling in organic solvents is established to have environmentally-dependent driving forces with significant activation barriers. We then demonstrate that mixing solvents and small molecules alter not only the driving forces to assembly, but also introduce high energy interfaces that impact kinetics and stimulate changes in polymer conformation. These changes are shown to be highly dependent upon the physicochemical properties of both the polymer and the interface. Our characterization, leveraging analysis techniques from both polymer physics and protein sciences, illuminates avenues for processing synthetic polymer assemblies in solution and provides an explanation for experimental observations of polymer interactions.