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. 2020 Jul 7;11:1010. doi: 10.3389/fphar.2020.01010

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Copyright © 2020 Gigolaev, Kuzmenkov, Peigneur, Tabakmakher, Pinheiro-Junior, Chugunov, Efremov, Tytgat and Vassilevski

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Production of MeKTx13-3 and its derivative. (A) Amino acid sequence alignment of MeKTx13-3 and MeKTx13-3_AAAR. Gray shading indicates the positions where replacements were introduced. Cysteine residues are in bold, and lines above the sequences indicate disulfide bonds. Take a note that recombinant analogue of MeKTx13-3 does not bear the C-terminal amidation of the natural toxin. (B, C) Reversed-phase HPLC separation of recombinant MeKTx13-3 and MeKTx13-3_AAAR after digestion by enteropeptidase. For target peptides the measured molecular masses are indicated.