Protein lipidation is a common post-translational modification (PTM) that controls the location and the function of proteins <i>in vivo</i>. We have previously demonstrated that lipidation can also be used to generate amphiphilic lipoproteins with controllable assembly <i>in vitro</i>. However, the repertoire of lipids in biology faces evolutionary constraints as the canonical lipidation machinery catalyzes the transfer of only a few types of lipids (saturated and unsaturated fatty acids, sterols, etc.) to recognized substrates.  To address this issue, we leveraged the substrate promiscuity of the lipidation machinery to incorporate artificial lipids into proteins, thus forming lipoproteins bearing a non-canonical PTM (ncPTM). We hypothesized that the distinct physical properties of these artificial lipids can be used to modulate the assembly of lipoproteins in a way that might differ from biological lipids. As a proof-of-concept, we leveraged the ability of N-myristoyltransferase to accept analogues of myristic acid. Our results demonstrate that these noncanonical lipoproteins self-assemble in solution, and they exhibit distinctive temperature-triggered emergent assembly that is absent in the canonical lipoprotein. Our study demonstrates the promise of expanding the repertoire of PTMs for the development of nanomaterials with unique assembly and function.

Non-canonical lipoproteins with emergent temperature-triggered assembly

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.