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Full-Text Articles in Life Sciences
Interactions Between Ions And Lysenin Nanochannels And Their Potential Applications As Biosensors, Radwan Awwad Al Faouri
Interactions Between Ions And Lysenin Nanochannels And Their Potential Applications As Biosensors, Radwan Awwad Al Faouri
Graduate Theses and Dissertations
Lysenin is classified as a pore-forming toxin protein that is isolated from the earthworm Eisenia fetida and consists of 297 amino acids [1]. Lysenin inserts large conducting pores (3.0-4.7 nm in diameter) into artificial membranes (BLM) which include sphingomyelin. These pores (channels) are open and oriented upon insertion into the bilayer lipid membrane. Lysenin channels gate at positive voltages (voltage-induced gating), but not at negative voltages. Lysenin pores also exhibit activity modulation in response to changes in ionic strength and pH, indicating that electrostatic interaction is responsible for Lysenin conductance activities. In this line of inquiries, and by modulating Lysenin …
Dynamics And Model Of The Pore-Forming Protein Lysenin, Eric Krueger
Dynamics And Model Of The Pore-Forming Protein Lysenin, Eric Krueger
Graduate Theses and Dissertations
Membrane transporters are a class of membrane proteins that function to provide a pathway across a cell membrane for the movement of ions and biomolecules. Investigations into the regulatory mechanism of these systems are hindered by their extensive preparation requirements compounded by their fragility and instability. However, lysenin, a pore-forming protein extracted from the earthworm Eisenia foetida, provided a unique opportunity to study a protein which is stable in both a soluble and membrane phase. Lysenin channels possess several important properties characteristic of ion channels without the inherent difficulties that plague investigations with biologically vital membrane transporters like voltage-gated ion …