Structural and biophysical properties of a synthetic channel-forming peptide: designing a clinically relevant anion selective pore.

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 NK(4)-M2

SUBMITTER: Bukovnik U 

PROVIDER: S-EPMC3245884 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature