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. 2020 Jun 5;11:688. doi: 10.3389/fphar.2020.00688

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Copyright © 2020 Ahmad, Saleem, Riaz, Lee, Diri, Noor, Almasri, Bagalagel and Elsebai

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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Structures of lynbyastatins, somamide B, Bouillomides, and kempopeptin A from different Lyngbya spp. They are cyclic depsipeptides containing Ahp unit; all (except kempopeptin A) having Abu unit neighbor to the Ahp unit. The Ahp residue contains a glutamate semi-aldehyde bonded as hemi-aminal to the amide nitrogen of the following aa; kempopeptin A is a new Ahp-containing depsipeptide and possessing N-acetylated Pro. The ester linkage for these depsipeptides was formed between a threonine OH group and the hydrophobic C-terminus of the precursor peptide.