(32h) Morphology of Enzyme-Random Heteropolymer Complexes

The decomposition of biodegradable plastics via nano-dispersed enzymes offers a promising solution to plastic pollution. The stabilization of enzymes using methacrylate-based random heteropolymers (RHPs) has shown potential in facilitating the degradation process. However, the mechanisms underlying RHP-facilitated enzyme stabilization remain unclear. This work focuses on understanding the morphology of the RHP-enzyme interaction, particularly with Proteinase K, known for its capability to degrade polyesters. By using biased and unbiased atomistic molecular dynamics simulations and machine learning, we explore the effect of different RHP compositions and initial conjugate structures, including globule-globule (‘polymer-enzyme dimer’) and coil-globule (‘polymer wrapping enzyme’) morphologies. The polymer globule in the dimer morphology interacts with the enzyme primarily through the side chain, and the backbone reconfiguration is hindered by the glassy nature of PMMA. The polymer coil in the wrapped morphology partially refolds, and further refolding is not favored. The preference for polymer-enzyme contacts correlates with the enzyme surface characterization and agrees with experimental results. We believe that the atomistic details of such conjugates are crucial for future material design and enzyme stabilization.