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Structurally Diverse μ‐Conotoxin PIIIA Isomers Block Sodium Channel Na V 1.4
Author(s) -
Tietze Alesia A.,
Tietze Daniel,
Ohlenschläger Oliver,
Leipold Enrico,
Ullrich Florian,
Kühl Toni,
Mischo André,
Buntkowsky Gerd,
Görlach Matthias,
Heinemann Stefan H.,
Imhof Diana
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201107011
Subject(s) - conotoxin , sodium channel , block (permutation group theory) , disulfide bond , chemistry , sodium , fragment (logic) , computer science , stereochemistry , biochemistry , combinatorics , algorithm , mathematics , peptide , organic chemistry
The one and only fold? Three chemically synthesized μ‐conotoxin PIIIA isomers (see picture), which contain different disulfide connectivity, block the skeletal muscle voltage‐gated sodium channel Na V 1.4 with similar, yet distinguishable potency. Hence, bioactivity of this μ‐conotoxin is not strictly coupled to its native fold. Future development of conotoxin‐derived analgesics may benefit from such a widened structural repertoire.