Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor m2 segment.

@article{Cook2004ActivityAS,
  title={Activity and structural comparisons of solution associating and monomeric channel-forming peptides derived from the glycine receptor m2 segment.},
  author={Gabriel A. Cook and Om Prakash and Ke Zhang and Lalida P Shank and Wade A Takeguchi and Ashley S Robbins and Yu-Xi Gong and Takeo Iwamoto and Bruce D. Schultz and John M Tomich},
  journal={Biophysical journal},
  year={2004},
  volume={86 3},
  pages={1424-35}
}
A number of channel-forming peptides derived from the second transmembrane (TM) segment (M2) of the glycine receptor alpha(1) subunit (M2GlyR), including the 22-residue sequence NK(4)-M2GlyR p22 wild type (WT) (KKKKPARVGLGITTVLTMTTQS), induce anion permeation across epithelial cell monolayers. In vitro assays suggest that this peptide or related sequences might function as a candidate for ion channel replacement therapy in treating channelopathies such as cystic fibrosis (CF). The wild-type… CONTINUE READING

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