Spontaneous Sequestration of Proteins into Liquid Crystalline Microdroplets

Abstract

Abstract In this work a facile method for fabricating protein‐sequestered liquid crystal (LC) emulsion droplets based on the uptake of surface‐engineered protein–polymer surfactant (PS) core–shell bioconjugates is described. Uptake of myoglobin‐PS, bovine serum albumin‐PS, Zn‐porphyrin myoglobin‐PS, horseradish peroxidase‐PS, and glucose oxidase‐PS occurs without structural or functional degradation, and gives rise to sequestration within the interior or at the surface of 4‐cyano‐4′‐pentylbiphenyl (5CB) nematic droplets depending on the surface modification of the protein‐PS bioconjugates. Differences in uptake behavior are used to achieve the spontaneous positional assembly of multiple proteins in the LC phase, and the use of spatially separated glucose oxidase‐PS and horseradish peroxidase‐PS bioconjugates is demonstrated to produce 5CB based droplets capable of housing an enzyme cascade reaction. This method opens a pathway for the development of bioactive liquid crystal droplets and can have potential applications in the optical sensing of biomolecular substrates.