Postdoc Seminar: From peptides to microcompartments: manipulating targets of different sizes with “protein” engineering

Amino acids comprise structures of various sizes, ranging from a short chain of a peptide to complex macromolecular assemblies. By modifying residues within peptides and proteins or proteins that make up the assemblies, we can gain insight into the modification target’s native function or enhance its function. In this talk, I will describe how I have successfully used protein engineering approaches to modify the properties of targets of different sizes, including an antimicrobial peptide (small), a fluorescent protein (medium), and a protein shell assembly (large). Starting at the peptide level, I first increased both the proteolytic resistance and the antifungal activity of the peptide histatin-5 against Candida albicans using rational design approach. Moving up in target size to proteins, I am enhancing the fluorescence of de novo designed mini-fluorescence-activating protein using the directed evolution approach. Finally, at the protein assembly level, we took steps forward in understanding the assembly of the protein shell of bacterial microcompartments in Salmonella enterica. Using that project's outcome, I have an ongoing work to produce medium-chain fatty acids by encapsulating the reverse beta-oxidation pathway within the microcompartments. My work in these diverse projects shows how protein engineering concepts can be applied to targets of different sizes in different organisms.

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