Figure 5 | Scientific Reports

Figure 5

From: Toxin acidic residue evolutionary function-guided design of de novo peptide drugs for the immunotherapeutic target, the Kv1.3 channel

Figure 5

Binding interfaces and non-binding interfaces of BmKTX-19 and BmKTX-196 identified by alanine-scanning mutagenesis.

A, Effects of BmKTX-19 and its alanyl mutants in blocking Kv1.3 channels. B, The circular dichroism spectra of recombinant peptides including BmKTX-19, BmKTX-19/K6A, BmKTX-19/K8A, BmKTX-19/H9A, BmKTX-19/K18A, BmKTX-19/K19A, BmKTX-19/R23A, BmKTX-19/K26A and BmKTX-19/N29A. C, Binding interface and non-binding interface of BmKTX-19; the key functional residues were marked blue. D, Effects of BmKTX-196 and its alanyl mutants in blocking Kv1.3 currents. E, The circular dichroism spectra of recombinant BmKTX-196, BmKTX-196/K8A, BmKTX-196/H9A, BmKTX-196/K15A, BmKTX-196/K18A, BmKTX-196/K19A, BmKTX-196/R23A and BmKTX-196/K26A peptides. F, Binding interface and non-binding interface of BmKTX-196; the key functional residues were marked blue.

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