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A mutant of the Buthus martensii Karsch antitumor-analgesic peptide exhibits reduced inhibition to hNa_v1.4 and hNa_v1.5 channels while retaining analgesic activity.

ABSTRACT: Scorpion toxins can kill other animals by inducing paralysis and arrhythmia, which limits the potential applications of these agents in the clinical management of diseases. Antitumor-analgesic peptide (AGAP), purified from Buthus martensii Karsch, has been proved to possess analgesic and antitumor activities. Trp³⁸, a conserved aromatic residue of AGAP, might play an important role in mediating AGAP activities according to the sequence and homology-modeling analyses. Therefore, an AGAP mutant, W38G, was generated, and effects of both AGAP and the mutant W38G were examined by whole-cell patch clamp techniques on the sodium channels hNa_v1.4 and hNa_v1.5, which were closely associated with the biotoxicity of skeletal and cardiac muscles, respectively. Th

SUBMITTER: Xu Y

PROVIDER: S-EPMC5672049 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

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A mutant of the Buthus martensii Karsch antitumor-analgesic peptide exhibits reduced inhibition to hNa_v1.4 and hNa_v1.5 channels while retaining analgesic activity.

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Dataset Information

A mutant of the Buthus martensii Karsch antitumor-analgesic peptide exhibits reduced inhibition to hNav1.4 and hNav1.5 channels while retaining analgesic activity.

OmicsDI is part of the ELIXIR infrastructure

Tweets

A mutant of the Buthus martensii Karsch antitumor-analgesic peptide exhibits reduced inhibition to hNa_v1.4 and hNa_v1.5 channels while retaining analgesic activity.