Membrane proteins are essential for a wide range of cellular functions, including enzymatic reactions, signal transduction, and selective transport of ions and molecules across the cell membrane. Their exceptional selectivity for a specific ion or molecule make them highly attractive for integration into synthetic host materials for various technological applications. However, effectively stabilizing functionally active membrane protein molecules at high concentrations in non-biological environments has been exceedingly challenging due to their intrinsic hydrophobicity and limited synthetic conditions to preserve their structural and functional integrities in abiotic hosts. Here, we demonstrate the incorporation of functionally active membrane proteins at high concentrations, up to 44 wt% protein, into robust, abiotic mesostructured silica-surfactant films for selective ion or molecular transport. Surfactants play a dual role, stabilizing membrane proteins via hydrophobic interactions while promoting co-assembly into ordered mesophases, with crosslinked silica providing mechanical stability to the resulting composite material. In particular, a tailored combination of non-ionic, cationic, and zwitterionic surfactants under ambient and mildly acidic conditions enables membrane protein-hybrid films to be prepared with high degrees of mesoscale order and uniform and tunable mesochannel dimensions, as established by small-angle X-ray scattering. Solid-state two-dimensional ²⁹Si{¹H} correlation NMR analyses reveal the molecular-scale interactions between the surfactant head groups and mesostructured silica surfaces, which points to the importance of surfactant species architecture and compositions to achieve both structure direction and protein stabilization. Furthermore, circular dichroism and UV-Visible spectroscopy demonstrate that the membrane proteins retain their secondary structures and functional activity within the silica-surfactant mesochannels, even at temperatures exceeding 100 °C. These findings establish key relationships between molecular composition, structure, and functionality of membrane proteins in abiotic inorganic-organic host environments, providing valuable insights for the design and synthesis of novel biomimetic materials for new separation applications.
