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. Author manuscript; available in PMC: 2022 Sep 14.
Published in final edited form as: Nat Chem Biol. 2022 Mar 14;18(5):511–519. doi: 10.1038/s41589-022-00981-0

Fig. 2 |. Activities of venom-insulin hybrid (Vh-Ins) analogs based on cone snail venoms containing extended A-chain sequences.

Fig. 2 |

a, Sequences of human insulin, human DOI and venom-DOI hybrids. Red letters indicate altered sequence relative to human insulin, X represents the elongated A chain sequences in Fig. 1c. b, Cellular activities of Vh-Ins analogs as assessed by pAKT in NIH 3T3 cells overexpressing IR-B (all with B10E, B20L substitutions) with various elongated A-chain sequences from cone-snail insulins (without C-terminal amidation). Error bars are shown when greater than the size of the symbols. c, Cellular activities of Vh-Ins analogs with alanine substitutions. All sequences are without C-terminal amidation.