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Eva Rose Balog, Ph.D., assistant professor of chemistry, co-authored an article titled “Genetically Engineered Elastomeric Polymer Network through Protein Zipper Assembly,” which was published in June 2017 in the journal ChemistrySelect.

The article describes the design, assembly, and characterization of a novel protein-based material. The material is formed via spontaneous self-assembly of two genetically engineered protein polymers. Each polymer, called a Helix-Elastin-Like-Polymer, or HELP, consists of two types of blocks: protein helical “zippers” that are programmed to pair in a specific way and short segments that resemble elastin, a stretchy protein that exhibits stimuli-responsive extension and contraction. The result of the self-assembly is a flexible two-dimensional meshwork with nanoscale pores. The pore size can change dynamically upon application of stimuli such as temperature. Such stimuli-responsive, “smart” materials may be useful in applications such as nanofabrication, tissue engineering and the development of biocompatible membranes with selective permeability.  

Balog and her co-researchers used the computational design tool Rosetta to predict and refine the pairwise protein interactions that define the assembly. Then they produced their designs using E. coli bacteria to manufacture the engineered protein polymers. Finally, they assembled the material from two HELPs and characterized the assembly using scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Their microscopy experiments showed the mesh-like structure of the HELP assembly with tunable pore sizes from around 16 to 32 nanometers (billionths of a meter), depending on the temperature.

The paper was co-authored with colleagues from Los Alamos National Laboratory’s Bioscience Division, Center for Integrated Nanotechnologies, and Institute for Material Science.

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