| Autor: |
Tomares DT; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States., Whitlock S; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States., Mann M; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States., DiBernardo E; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States., Childers WS; Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States. |
| Abstrakt: |
Peptide nanomaterials exhibit diverse applications in vitro, such as drug delivery. Here, we consider the utility of de novo peptide nanomaterials to organize biochemistry within the bacterial cytoplasm. Toward this goal, we discovered that ABC coiled-coil triblock peptides form gel-like biomolecular condensates with a c sat of 10 μM in addition to their well-known hydrogel-forming capabilities. Expression of the coiled-coil triblock peptides in bacteria leads to cell pole accumulation via a nucleoid occlusion mechanism. We then provide a proof of principle that these synthetic biomolecular condensates could sequester clients at the cell pole. Finally, we demonstrate that triblock peptides and another biomolecular condensate, RNase E, phase-separate as distinct protein-rich assemblies in vitro and in vivo. These results reveal the potential of using peptide nanomaterials to divide the bacterial cytoplasm into distinct subcellular zones with future metabolic engineering and synthetic biology applications. |
