Genetically engineered proteins have made a significant impact in biomaterials research enabling the fabrication of polymers with monodisperse molecular weights, a diverse set of side chain functionality and well-defined secondary structure elements. Advances in unnatural amino acid incorporation, with a particular focus on fluorinated amino acids, enable the integration of chemical diversity into such proteins, further expanding the level of control of materials properties. Recently, we have demonstrated that protein block polymers consisting of two self-assembling domains (SADs), derived from elastin (E) and the coiled-coil domain of COMP (C), in the configurations EC, CE and ECE, exhibit distinct modes of assembly. The SAD arrangements and quantity within a single protein polymer chain essentially impacts the structure, supramolecular assembly and mechanical properties. Here we explore the effects of incorporating para-fluorophenylalanine (pFF), into the protein block polymer sequences to produce pFF-EC, pFF-CE, and pFF-ECE in an attempt to modulate overall physicochemical properties.

Modulating supramolecular assemblies and mechanical properties of engineered protein materials by fluorinated amino acids

243rd National Meeting (2012)

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