Post-translational modification of proteins is a common strategy in biological systems to expand the diversity of proteomes and to tailor the function and location of proteins in a cellular environment. Advances in analytical techniques have resulted in rapid expansion of our knowledge of post-translational modification machinery and targets. Nonetheless, harnessing these diverse modifications for the purpose of building novel hybrid biomaterials has remained an underexplored territory in materials science and engineering for two reasons. Firstly, most protein-based materials are currently produced in E. coli, a prokaryote lacking many of the advanced post-translational modification machinery. Secondly, facile and scalable separation of unmodified proteins from the post-transitionally modified products is often challenging. To address these issues and as a proof of concept, we utilized a co-expression strategy to simultaneously express a eukaryotic lipid transferase and an elastin-like polypeptide (ELP) substrate in E. coli using bicistronic expression systems. ELP substrate is used as a model polymer with well-defined composition and length, allowing for inexpensive and scalable purification of modified and unmodified products through its thermally-triggered phase transition. We demonstrate that it is possible to produce precise and well-defined hybrid lipid-protein-based materials in a simple one-pot expression system using this strategy. More importantly, these novel hybrid biomaterials are promising candidates for biomedical applications, as it is possible to program their function by controlling their self-assembly across many length scale by rationally tuning the lipid and polypeptide sequence.

Genetically encoded lipid-polypeptide hybrid biomaterials

253rd National Meeting (2017)

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