The present study shows that a cyclic peptide has a great specificity to interact with a specific homolog of a highly conserved protein family. Summary: When alpha lawyer Viktor Nikiforov is given the case of omega Katsuki Yuuri, accused of second-degree murder, he wasn’t expecting the emotional turmoil he was currently dragged into. Triggers: Anxiety, PTSD, Panic Attacks, Rape/Non-Con. These results indicate that surfactin inhibits the cellular function of Hsp90 specifically in the cyanobacterium. Pairing: Katsuki Yuuri/Viktor Nikiforov Status: Ongoing. Surfactin did not show significant cellular toxicity towards mammalian cells.

Surfactin also inhibited the interaction of the cyanobacterial Hsp90 with a model substrate, and suppressed S.elongatus growth under heat stress, but not that of E.coli. The data suggest that surfactin inhibits a rate-limiting conformational change of S.elongatus Hsp90 in the ATP hydrolysis. Molecular docking simulations indicated that surfactin could bind to the N-terminal dimerization interface of the cyanobacterial Hsp90 in the ATP- and ADP-bound states, which provided molecular insights into the species-selective inhibition.

We found that a cyclic lipopeptide surfactin inhibits the ATPase activity of Hsp90 from the cyanobacterium Synechococcus elongatus ( S.elongatus) PCC 7942 but does not inhibit Escherichia coli ( E.coli), yeast and human Hsp90s. Identifying species-specific Hsp90 inhibitors is challenging because Hsp90 is evolutionarily conserved. Heat shock protein 90 (Hsp90) is essential for eukaryotic cells, whereas bacterial homologs play a role under stresses and in pathogenesis.

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