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- W1970251145 abstract "CFTR (cystic fibrosis transmembrane conductance regulator) is an epithelial Cl− channel inhibited with high affinity and selectivity by the thiazolidinone compound CFTRinh-172. In the present study, we provide evidence that CFTRinh-172 acts directly on the CFTR. We introduced mutations in amino acid residues of the sixth transmembrane helix of the CFTR protein, a domain that has an important role in the formation of the channel pore. Basic and hydrophilic amino acids at positions 334–352 were replaced with alanine residues and the sensitivity to CFTRinh-172 was assessed using functional assays. We found that an arginine-to-alanine change at position 347 reduced the inhibitory potency of CFTRinh-172 by 20–30-fold. Mutagenesis of Arg347 to other amino acids also decreased the inhibitory potency, with aspartate producing near total loss of CFTRinh-172 activity. The results of the present study provide evidence that CFTRinh-172 interacts directly with CFTR, and that Arg347 is important for the interaction." @default.
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- W1970251145 date "2008-06-12" @default.
- W1970251145 modified "2023-10-14" @default.
- W1970251145 title "Evidence for direct CFTR inhibition by CFTRinh-172 based on Arg347 mutagenesis" @default.
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- W1970251145 doi "https://doi.org/10.1042/bj20080029" @default.
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