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The solvent quality determines the collapsed or the expanded state of apolymer. For example, a polymer dissolved in a poor solvent collapses, whereasin a good solvent it opens up. While this standard understanding is generallyvalid, there are examples when a polymer collapses even in a mixture of twogood solvents. This phenomenon, commonly known as co-non-solvency, is usuallyassociated with smart polymers. Moreover, recent experiments have shown thatthe elastin-like polypeptides (ELPs) show co-non-solvency behavior inaqueous-ethanol mixtures. In this study, we investigate the phase behavior ofELPs in aqueous binary mixtures using molecular dynamics simulations ofall-atom and complementary explicit solvent generic models. The model isparameterized by mapping the solvation free energy obtained from the all-atomsimulations onto the generic interaction parameters. For this purpose, wederive segment based generic parameters for four different peptides, namelyproline (P), valine (V), glycine (G) and alanine (A). Here we compare theconformational behavior of two ELP sequences, namely VPGGG and VPGVG, inaqueous-ethanol and -urea mixtures. Consistent with recent experiments, we findthat ELPs show co-non-solvency in aqueous-ethanol mixtures. Ethanol moleculeshave preferential binding with all ELP residues and thus driving thecoil-to-globule transition. On the contrary, ELP conformations show weakvariation in aqueous-urea mixtures. Our simulations suggest that the glycineresidues dictate the overall behavior of ELPs in aqueous-urea, where ureamolecules have a rather weak preferential binding with glycine, i.e., less thankT. While the validation of the latter findings will require more detailedexperimental investigation, the results presented here may provide a new twistto the present understanding of cosolvent interactions with peptides andproteins.

Why Do Elastin-Like Polypeptides Possibly Have Different Solvation Behaviors in Water-Ethanol and Water-Urea Mixtures?