A Simple Generic Model of Elastin-Like Polypeptides with Proline Isomerization

A generic model of elastin-like polypeptides (ELP) is derived that includes proline isomerization (ProI). As a case study, conformational transition of a -[valine-proline-glycine-valine-glycine]- sequence is investigated in aqueous ethanol mixtures. While the non-bonded interactions are based on the Lennard-Jones (LJ) parameters, the effect of ProI is incorporated by tuning the intramolecular 3- and 4-body interactions known from the underlying all-atom simulations into the generic model. One of the key advantages of such a minimalistic model is that it readily decouples the effects of geometry and the monomer-solvent interactions due to the presence of ProI, thus gives a clearer microscopic picture that is otherwise rather nontrivial within the all-atom setups. These results are consistent with the available all-atom and experimental data. The model derived here may pave the way to investigate large scale self-assembly of ELPs or biomimetic polymers in general. Understanding the solvation behavior of elastin-like polypeptides is crucial in designing high-performance biomaterials for their advanced functional applications. In this work, a simple generic model is derived to investigate the effect of proline isomerization on ELP conformations in binary mixtures. The far-reaching implication of such a simplistic model might be to study the large scale self-assembly of biomolecules. image