Figure 7: Pore selectivities and conductivities. | Nature Communications

Figure 7: Pore selectivities and conductivities.

From: Spontaneous formation of structurally diverse membrane channel architectures from a single antimicrobial peptide

Figure 7

(a–c) Higher-order oligomeric channel-like structures (hexamers, heptamers and octamers) were taken from the pore assembly simulation and equilibrated in a separate lipid bilayer. Water flow and conductance of Na, K and Cl ions were measured from simulations with applied voltages. No restraints were required and the pores remained stable over the 4 μs timescale of the simulations (Supplementary Table 2). (d) Conduction and (e) water flux are dominated by the large higher-order oligomeric pores (that is, >5 peptides), which were found to be consistent in pore size with the macromolecule vesicle leakage pore-sizing assay (Fig. 1). Pores show a preference for conducting anions (Cl) over cations, and K+ conducts roughly 2–3 times the rate of Na+.

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