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• W1900553567 abstract "Nanopores based on protein channels inserted into lipid membranes have paved the way towards a wide-range of inexpensive biosensors, especially for DNA sequencing. A key obstacle in using these biological ion channels as nanodevices is the poor stability of lipid bilayer membranes. Amphiphilic block copolymer membranes have emerged as a robust alternative to lipid membranes. While previous efforts have shown feasibility, we demonstrate for the first time the effect of polymer composition on MspA protein functionality. We show that membrane-protein interaction depends on the hydrophobic-hydrophilic ratio (f-ratio) of the block copolymer. These effects are particularly pronounced in asymmetric protein pores like MspA compared to the cylindrical α-Hemolysin pore. A key effect of membrane-protein interaction is the increased 1/fα noise. After first showing increases in 1/fα behaviour arise from increased substate activity, the noise power spectral density S(f) was used as a qualitative tool for understanding protein-membrane interactions in polymer membranes. Polymer compositions with f-ratios close to lipid membranes caused noise behaviour not observed in lipid membranes. However, by modifying the f-ratio using a modular synthetic approach, we were able to design a block copolymer exhibiting noise properties similar to a lipid membrane, albeit with better stability. Thus, by careful optimization, block copolymer membranes can emerge as a robust alternative for protein-pore based nano-biosensors." @default.
• W1900553567 created "2016-06-24" @default.
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• W1900553567 date "2015-01-01" @default.
• W1900553567 modified "2023-09-27" @default.
• W1900553567 title "Tailored polymeric membranes for Mycobacterium smegmatis porin A (MspA) based biosensors" @default.
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• W1900553567 doi "https://doi.org/10.1039/c5tb00383k" @default.
• W1900553567 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4582436" @default.
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