'Messy' Processing of χ-conotoxin MrIA Generates Homologues with Reduced hNET Potency.

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ID: 26404
2019
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Abstract
Integrated venomics techniques have shown that variable processing of conotoxins from resulted in a dramatic expansion in the number of expressed conotoxins. One conotoxin from , the χ-conotoxin MrIA, is a selective inhibitor of human norepinephrine transporters (hNET) and therefore a drug candidate for attenuating chronic neuropathic pain. It has been found that "messy" processing of the MrIA transcripts results in the expression of MrIA analogs with different truncations of the pro-peptide that contains portions of the MrIA molecule. The aim of this study was to investigate if variable processing of the expressed peptides results in modulation of the existing hNET pharmacology or creates new pharmacologies. To this end, a number of MrIA analogs found in venom were synthesized and evaluated for their activity at hNET receptors. While several of the analogs exhibited norepinephrine transporter inhibitory activity comparable to that of MrIA, none significantly improved on the potency of conotoxin MrIA, and those analogs with disrupted pharmacophores produced greatly reduced NET inhibition, confirming previous structure-activity relationships seen on χ-class conopeptides. Additionally, analogs were screened for new activities on ion channels using calcium influx assays, although no major new pharmacology was revealed.
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ziegman2019messymarine Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ziegman, Rebekah;Brust, Andreas;Jha, Prerna;Cardoso, Fernanda C;Lewis, Richard J;Alewood, Paul F;
Journal Marine drugs
Year 2019
DOI
E165
URL
Keywords Keywords not found

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