Bio-Inspired Random Heteropolymers

A new class of bio-inspired PMMA-based random heteropolymers (RHPs) have displayed versatile protein-like properties, including catalytic activities, transporting protons across a bilayer lipid membrane, and protecting protein in a non-native environment. By using atomistic molecular dynamics simulation, these RHP chains collapse into compact globules, and the hydration of monomers is frustrated. The interaction with a hydrophobic substrate (i.e., graphene and its derivatives) and a β-barrel protein is driven by the ethylene glycol side chains, and the adsorption is hindered by the glassy PMMA backbone architecture and substrate hydrophilicity. These protein-like properties, including compactness, hydration frustration, and protein stabilization through heterodimerization are sequence-insensitive, which is not generally held for other similar backbone architectures. The design of PMMA-based RHP provides an alternative orthogonal to the sequence-structure-function paradigm of the protein.