Affiliation: | 1. Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99354 USA Materials Science and Engineering, University of Washington, Seattle, WA, 98105 USA;2. Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99354 USA;3. Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, CA, 94550 USA;4. Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, CA, 94550 USA School of Natural Sciences, University of California Merced, Merced, CA, 95343 USA;5. Department of Chemical Engineering, University of Washington, Seattle, WA, 98105 USA;6. Materials Science and Engineering, University of Washington, Seattle, WA, 98105 USA;7. Physical Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99354 USA Department of Chemical Engineering, University of Washington, Seattle, WA, 98105 USA |
Abstract: | Robust and cost-effective membrane-based separations are essential to solving many global crises, such as the lack of clean water. Even though the current polymer-based membranes are widely used for separations, their performance and precision can be enhanced by using a biomimetic membrane architecture that consists of highly permeable and selective channels embedded in a universal membrane matrix. Researchers have shown that artificial water and ion channels, such as carbon nanotube porins (CNTPs), embedded in lipid membranes can deliver strong separation performance. However, their applications are limited by the relative fragility and low stability of the lipid matrix. In this work, we demonstrate that CNTPs can co-assemble into two dimension (2D) peptoid membrane nanosheets, opening up a way to produce highly programmable synthetic membranes with superior crystallinity and robustness. A combination of molecular dynamics (MD) simulations, Raman spectroscopy, X-ray diffraction (XRD), and atomic force microscopy (AFM) measurements to verify the co-assembly of CNTP and peptoids are used and show that it does not disrupt peptoid monomer packing within the membrane. These results provide a new option for designing affordable artificial membranes and highly robust nanoporous solids. |