LAUSR

AbstractPost-translational modification of proteins is a strategy widely used in biological systems. It expands the diversity of the proteome and allows for tailoring of both the function and localization of proteins within cells as well as the material properties of structural proteins and matrices. Despite their ubiquity in biology, with a few exceptions, the potential of post-translational modifications in biomaterials synthesis has remained largely untapped. As a proof of concept to demonstrate the feasibility of creating a genetically encoded biohybrid material through post-translational modification, we report here the generation of a family of three stimulus-responsive hybrid materials—fatty-acid-modified elastin-like polypeptides—using a one-pot recombinant expression and post-translational lipidation methodology. These hybrid biomaterials contain an amphiphilic domain, composed of a β-sheet-forming peptide that is post-translationally functionalized with a C14 alkyl chain, fused to a thermally responsive elastin-like polypeptide. They exhibit temperature-triggered hierarchical self-assembly across multiple length scales with varied structure and material properties that can be controlled at the sequence level.Inspired by the post-translational modifications of polypeptides widespread in biological systems, the one-pot synthesis of biohybrid materials was engineered within Escherichia coli using a recombinant expression and post-translational lipidation. The fatty-acid-modified elastin-like polypeptides (FAMEs) prepared, which comprise peptide-amphiphile segments prone to self-assembly fused to a thermally responsive elastin-like polypeptide, exhibit temperature-triggered hierarchical assembly.