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Crystallographic structure of a helical lipopeptaibol antibiotic analogue

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Summary

An X-ray diffraction analysis of the [Fmoc0, TOAC4,8, Leu-OMe11]analogue of the lipopeptaibol antibiotic trichogin A Iv shows that the undecapeptide is folded in a right-handed, mixed α/310-helix. The helical molecules are connected in a head-to-tail arrangement along the b-axis through C=O...H-N intermolecular H-bonding. This packing mode generates a hydrophobic cavity where the Fmoc Nα-protecting groups are accommodated. The distances and angles between the nitroxide groups of the two TOAC residues, separated by one turn of the α-helix, have been determined.

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Crisma, M., Monaco, V., Formaggio, F. et al. Crystallographic structure of a helical lipopeptaibol antibiotic analogue. Lett Pept Sci 4, 213–218 (1997). https://doi.org/10.1007/BF02442878

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