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. 2020 Jul 8;11:991. doi: 10.3389/fphar.2020.00991

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Copyright © 2020 Osmakov, Khasanov, Andreev, Lyukmanova and Kozlov

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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The influence of point mutation in polypeptide modulators on modulating activity to ASICs. Mutations without effect (green), medium affecting (yellow), and destroy the activity (orange) distributed in accordance with publications (references shown in picture). The decrease of mutants’ functional activity as part of the wild-type peptide activity for each substitution is presented below as a number except for: X1, loss of ability to inhibit ASICs; X2, loss of ability to inhibit rASIC1a at low concentration and gain of function as a positive modulator at high concentrations (>100 nM); X3, 2,600-fold decrease in inhibition of rASIC1a, and inhibition becomes fully reversible; X4, important decrease in inhibitory potency on cASIC1a; X5 more than 100-fold decrease in ability to inhibit rASIC3; N1, small increase in inhibitory potency on cASIC1a.