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• W2057007235 abstract "The design, synthesis, modeling and in vitro testing of channel-forming peptides derived from the cys-loop superfamily of ligand-gated ion channels are part of an ongoing research focus. Over 300 different sequences have been prepared based on the M2 transmembrane segment of the spinal cord glycine receptor α-subunit. A number of these sequences are water-soluble monomers that readily insert into biological membranes where they undergo supramolecular assembly, yielding channels with a range of selectivities and conductances. Selection of a sequence for further modifications to yield an optimal lead compound came down to a few key biophysical properties: low solution concentrations that yield channel activity, greater ensemble conductance, and enhanced ion selectivity. The sequence NK4-M2GlyR T19R, S22W (KKKKPARVGLGITTVLTMRTQW) addressed these criteria. The structure of this peptide has been analyzed by solution NMR as a monomer in detergent micelles, simulated as five-helix bundles in a membrane environment, modified by cysteine-scanning and studied for insertion efficiency in liposomes of selected lipid compositions. Taken together, these results define the structural and key biophysical properties of this sequence in a membrane. This model provides an initial scaffold from which rational substitutions can be proposed and tested to modulate anion selectivity. This article is part of a Special Issue entitled: Protein Folding in Membranes." @default.
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• W2057007235 date "2012-04-01" @default.
• W2057007235 modified "2023-09-27" @default.
• W2057007235 title "Structural and biophysical properties of a synthetic channel-forming peptide: Designing a clinically relevant anion selective pore" @default.
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• W2057007235 doi "https://doi.org/10.1016/j.bbamem.2011.07.037" @default.
• W2057007235 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3245884" @default.
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