PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore

PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore. Chowdhury, R., Ren, T., Shankla, M., Decker, K., Grisewood, M., Prabhakar, J., Baker, C., Golbeck, J., H., Aksimentiev, A., Kumar, M., & Maranas, C., D. Nature Communications, 2018.

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PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore [link]

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Monodispersed angstrom-size pores embedded in a suitable matrix are promising for highly selective membrane-based separations. They can provide substantial energy savings in water treatment and small molecule bioseparations. Such pores present as membrane proteins (chiefly aquaporin-based) are commonplace in biological membranes but difficult to implement in synthetic industrial membranes and have modest selectivity without tunable selec-tivity. Here we present PoreDesigner, a design workflow to redesign the robust beta-barrel Outer Membrane Protein F as a scaffold to access three specific pore designs that exclude solutes larger than sucrose (>360 Da), glucose (>180 Da), and salt (>58 Da) respectively. PoreDesigner also enables us to design any specified pore size (spanning 3-10 Å), engineer its pore profile, and chemistry. These redesigned pores may be ideal for conducting sub-nm aqueous separations with permeabilities exceeding those of classical biological water channels , aquaporins, by more than an order of magnitude at over 10 billion water molecules per channel per second.

@article{
 title = {PoreDesigner for tuning solute selectivity in a robust and highly permeable outer membrane pore},
 type = {article},
 year = {2018},
 websites = {www.nature.com/naturecommunications},
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 abstract = {Monodispersed angstrom-size pores embedded in a suitable matrix are promising for highly selective membrane-based separations. They can provide substantial energy savings in water treatment and small molecule bioseparations. Such pores present as membrane proteins (chiefly aquaporin-based) are commonplace in biological membranes but difficult to implement in synthetic industrial membranes and have modest selectivity without tunable selec-tivity. Here we present PoreDesigner, a design workflow to redesign the robust beta-barrel Outer Membrane Protein F as a scaffold to access three specific pore designs that exclude solutes larger than sucrose (>360 Da), glucose (>180 Da), and salt (>58 Da) respectively. PoreDesigner also enables us to design any specified pore size (spanning 3-10 Å), engineer its pore profile, and chemistry. These redesigned pores may be ideal for conducting sub-nm aqueous separations with permeabilities exceeding those of classical biological water channels , aquaporins, by more than an order of magnitude at over 10 billion water molecules per channel per second.},
 bibtype = {article},
 author = {Chowdhury, Ratul and Ren, Tingwei and Shankla, Manish and Decker, Karl and Grisewood, Matthew and Prabhakar, Jeevan and Baker, Carol and Golbeck, John H and Aksimentiev, Aleksei and Kumar, Manish and Maranas, Costas D},
 doi = {10.1038/s41467-018-06097-1},
 journal = {Nature Communications}
}

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