Structurally Diverse μ‐Conotoxin PIIIA Isomers Block Sodium Channel Na V 1.4 | Zendy

Tietze Alesia A. | Zendy; Tietze Daniel | Zendy; Ohlenschläger Oliver | Zendy; Leipold Enrico | Zendy; Ullrich Florian | Zendy; Kühl Toni | Zendy; Mischo André | Zendy; Buntkowsky Gerd | Zendy; Görlach Matthias | Zendy; Heinemann Stefan H. | Zendy; Imhof Diana | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research