Diffusion of Proteins across Silica Colloidal Crystals
| Autor: | Robert Haynes, Patricia Anne A. Ignacio-de Leon, Ilya Zharov, Yulia Eygeris |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Materials science
Diffusion Sintering 02 engineering and technology 010402 general chemistry 01 natural sciences Tortuosity Hemoglobins Nanopores Colloid Electrochemistry Animals General Materials Science Colloids Particle Size Bovine serum albumin Spectroscopy biology Serum Albumin Bovine Surfaces and Interfaces Colloidal crystal Silicon Dioxide 021001 nanoscience & nanotechnology Condensed Matter Physics 0104 chemical sciences Nanopore Chemical engineering biology.protein Cattle Muramidase Adsorption 0210 nano-technology Selectivity Chickens |
| Zdroj: | Langmuir. 34:10333-10339 |
| ISSN: | 1520-5827 0743-7463 |
| DOI: | 10.1021/acs.langmuir.8b01261 |
| Popis: | We studied the diffusion of three model proteins, lysozyme (Lz), bovine hemoglobin (BHb), and bovine serum albumin (BSA), normal to the (111) plane of sintered silica colloidal crystals with three different pore "radii" (7.5, 19, and 27 nm). We demonstrated that these colloidal crystals exhibit size selectivity when the nanopores are sufficiently small (7.5 and 19 nm). Because these nanopores are still larger than the diffusing proteins, the observed size selectivity can be attributed to the tortuosity of the colloidal nanopores. Larger (27 nm) nanopores led to higher transport rates but at the cost of selectivity. In addition to the size selectivity, we also demonstrated that 19 nm nanopores possess shape selectivity for the proteins of comparable molecular weights. We showed that the high temperature sintering required for the preparation of sintered colloidal crystals reduces the extent of interactions between the proteins and the nanopore surface, which appear to play a minor role in the diffusion, and that transport selectivity is decided solely by protein size and shape. Taken together, our observations suggest that sintered silica colloidal crystals constitute promising nanoporous membranes for protein separations, with easily controllable pore size, size and shape selectivity, and minimal surface fouling. |
| Databáze: | OpenAIRE |
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