Sequence-(in)dependence protein-mimetic polymer

A new class of MMA-based random heteropolymers (RHPs) have displayed protein-like properties in an ensemble manner. Using atomistic molecular dynamics simulation, we have shown that the chain collapsed into globules with a weak sequence control. In this work, we find the sequence for MMA-based random heteropolymers do not contribute to the statistical properties of the monomers with different chemistries. However, this changes dramatically when we substitute the MMA backbone by a methacrylate (MA) backbone or by simply replacing the oxygen atom on the side chain with a nitrogen atom (methyl methacrylamide, MMAn or methacrylamide, MAn). In such a scenario, we find that the sequence is significant for the overall structure of the random copolymer. We apply the dimensionality reduction on the hydration of each monomer and find that in the case of MA and MAn/MMAn backbones, different sequences do not share any common space, meaning their properties are controlled by their sequence and not the composition which is maintained fixed. The sequence-independence of MMA-based RHPs provide a paradigm for protein-mimetic materials.