Engineering the Repeats-in-Toxin Domain for Biotechnology Applications

TL;DRAbstract

Repeat peptide domains are ubiquitous in nature. They consist of tandem repeats of a consensus sequence and are involved in a very wide array of different functions. The predictability of their sequence and, thus, their secondary structure has made them appealing scaffolds to bioengineers. A number of commonly found motifs have been subjected to bioengineering work aimed at consensus design. Such work focuses on identifying a modular repeat unit that can be multiplied as necessary to create a functional interface for applications such as creating novel biomolecular interactions or biomaterials. To be successful, a thorough understanding of the target motif must be obtained. One must understand what amino acids can be targeted for engineering and which are critical for proper folding. In this dissertation we describe our efforts to develop a new scaffold for biotechnology applications based on the beta roll forming repeats-in-toxin (RTX) domain. Unlike existing scaffolds, which tend to

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