ABSTRACT

Our group is inspired by Nature’s strategy of folding biopolymers into specific protein and RNA structures to build a toy model of a chain of droplets, i.e. “colloidomers”, that are designed via DNA interactions to fold into well-defined architectures. Indeed, simple alternating chains (up to 14 droplets long) with only two droplet flavors (ABABAB…) are sufficient to uniquely encode a dozen “foldamers”, constituting 1% of all possible rigid structures in 2D. Subsequently, these 2D foldamers can self-assemble into larger nets that, upon density-matching, are able to further fold into unique 3D geometries, e.g. an icosahedron. These hierarchical protocols circumvent the vast phase space of the nominal folding landscape, in which a random cluster of 12 particles has tens of thousands or rigid folds to choose from. Once the colloidal protein analog is formed, it can then be further programmed by the polymerase-exonuclease-nickase (PEN) toolbox of enzymes that interact with droplet-droplet DNA bonds, to produce highly non-linear dynamic systems. These “mayonnaise robots” promise to offer a bright and functional future on the colloidal length scale.