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Biomacromolecules. 2012 Aug 13;13(8):2273-8. doi: 10.1021/bm3005116. Epub 2012 Jul 24.

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

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Department of Chemical and Biological Sciences, Polytechnic Institute of NYU, Brooklyn, New York 11201, United States.


Here we describe the biosynthesis and characterization of fluorinated protein block polymers comprised of the two self-assembling domains (SADs): elastin (E) and the coiled-coil region of cartilage oligomeric matrix proteins (C). Fluorination is achieved by residue-specific incorporation of p-fluorophenylalanine (pFF) to create pFF-EC, pFF-CE, and pFF-ECE. Global fluorination results in downstream effects on the temperature-dependent secondary structure, supramolecular assembly, and bulk mechanical properties. The impact of fluorination on material properties also differs depending on the orientation of the block configurations as well as the number of domains in the fusion. These studies suggest that integration of fluorinated amino acids within protein materials can be employed to tune the material properties, especially mechanical integrity.

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