Abstract: A new class of sensing elements made of a protein pore fused to a programmable antibody-mimetic binder. This modular design expands the utility of nanopore sensors to numerous proteins while preserving their architecture, specificity, and sensitivity. The sensing elements were validated with protein analytes that drastically vary in size, charge, and structural complexity. These analytes produce unique electrical signatures that depend on their identity and quantity and the binder-analyte assembly at the nanopore tip.

Abstract: A bioinspired protein pore-based nanostructure that can provide selective, real-time sampling of protein-protein interactions at single-molecule resolution. This modular nanostructure relied on a single polypeptide chain that encompassed a heavily truncated outer membrane protein, a highly flexible connector, a protein receptor element, as well as a polypeptide adapter. The presence of a protein ligand analyte in solution produced reversible binding and release events, in the form of discrete and stochastic current transitions between open substates of the transmembrane pore, the nature of which depend on both the amount of protein ligand analyte and the strength of the transient PPIs in aqueous phase.

Abstract: A bioinspired protein pore-based nanostructure that can provide selective, real-time sampling of protein-protein interactions at single-molecule resolution. This modular nanostructure relied on a single polypeptide chain that encompassed a heavily truncated outer membrane protein, a highly flexible connector, a protein receptor element, as well as a polypeptide adapter. The presence of a protein ligand analyte in solution produced reversible binding and release events, in the form of discrete and stochastic current transitions between open substates of the transmembrane pore, the nature of which depend on both the amount of protein ligand analyte and the strength of the transient PPIs in aqueous phase.

Abstract: A mutant Escherichia coli ?-barrel monomeric protein pore bioengineered to remove a lumen-occluding domain and modify some of its extracellular domains. The modified protein, FhuA ?/C?4L, forms a highly conductive pore as compared to other known pores and is capable of sensing large polypeptides and discriminating between modified protein analytes.

Abstract: A mutant Escherichia coli ?-barrel monomeric protein pore bioengineered to remove a lumen-occluding domain and modify some of its extracellular domains. The modified protein, FhuA ?/C?4L, forms a highly conductive pore as compared to other known pores and is capable of sensing large polypeptides and discriminating between modified protein analytes.

Abstract: Provided are pore-subunit polypeptides covalently linked to one or more sensing moieties, and uses of these modified polypeptides to detect and/or measure analytes or physical characteristics within a given sample.

Abstract: Provided are pore-subunit polypeptides covalently linked to one or more sensing moieties, and uses of these modified polypeptides to detect and/or measure analytes or physical characteristics within a given sample.

Abstract: Provided are pore-subunit polypeptides covalently linked to one or more sensing moieties, and uses of these modified polypeptides to detect and/or measure analytes or physical characteristics within a given sample.