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Journal Article

Robust and long-term cellular protein and enzymatic activity preservation in biomineralized mammalian cells


Amini,  Shahrouz       
Shahrouz Amini, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Guo, J., Amini, S., Lei, Q., Ping, Y., Agola, J. O., Wang, L., et al. (2022). Robust and long-term cellular protein and enzymatic activity preservation in biomineralized mammalian cells. ACS Nano, 16(2), 2164-2175. doi:10.1021/acsnano.1c08103.

Cite as: https://hdl.handle.net/21.11116/0000-000A-0A32-3
Preservation of evolved biological structure and function in robust engineering materials is of interest for storage of biological samples before diagnosis and development of vaccines, sensors, and enzymatic reactors and has the potential to avoid cryopreservation and its associated cold-chain issues. Here, we demonstrate that "freezing cells in amorphous silica" is a powerful technique for long-term preservation of whole mammalian cell proteomic structure and function at room temperature. Biomimetic silicification employs the crowded protein microenvironment of mammalian cells as a catalytic framework to proximally transform monomeric silicic acid into silicates forming a nanoscopic silica shell over all biomolecular interfaces. Silicification followed by dehydration preserves and passivates proteomic information within a nanoscale thin silica coating that exhibits size selective permeability (<3.6 nm), preventing protein leaching and protease degradation of cellular contents, while providing access of small molecular constituents for cellular enzymatic reaction. Exposure of dehydrated silicified cells to mild etchant or prolonged hydrolysis removes the silica, completely rerevealing biomolecular components and restoring their accessibility and functionality.