Recombinant expression of proteins has emerged as a powerful strategy to access “precision polymers”, offering superb control over the sequence and the length of the final product. However, the precision offered by these recombinant methods is partially offset by the limited repertoire of monomers (canonical amino acids) and linkage chemistry (amide bond). Biology has overcome this limitation ingeniously by modifying proteins after expression using a diverse set of chemical transformations, post-translational modifications (PTMs). PTMs can significantly alter the function, localization and assembly of proteins in biological systems. Additionally, PTMs can be used to decorate proteins with diverse chemical moieties thus expanding the chemical and structural diversity of protein-based materials. Despite these obvious benefits, materials science and engineering community has not fully utilized the power of these diverse modifications to create new hybrid biomaterial.<br/>As a proof of concept, we have recently demonstrated that it is possible to produce precise and well-defined hybrid lipid-protein conjugates, Fatty Acid Modified Elastin-like polypeptides (FAME), in <i>E. coli</i> using a simple one-pot expression system. In this presentation, I discuss our progress toward expanding these modifications to more complex lipids such as sterols. These new hybrid biomaterials are thermally responsive and exhibit temperature-triggered hierarchical self-assembly across multiple length scales with varied structure and material properties that can be tuned at the sequence level.

Harnessing the power of post-translational modifications for materials science and engineering

254th National Meeting (2017)

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