Connecting the conformational behavior of cyclic octadepsipeptides with their ionophoric property and membrane permeability.

ABSTRACT: Cyclic octadepsipeptides such as PF1022A and its synthetic derivative emodepside exhibit anthelmintic activity with the latter sold as a commercial drug treatment against gastrointestinal nematodes for animal health use. The structure-permeability relationship of these cyclic depsipeptides that could ultimately provide insights into the compound bioavailability is not yet well understood. The fully N-methylated amide backbone and apolar sidechain residues do not allow for the formation of intramolecular hydrogen bonds, normally observed in the membrane-permeable conformations of cyclic peptides. Hence, any understanding gained on these depsipeptides would serve as a prototype for future design strategies. In previous nuclear magnetic resonance (NMR) studies, two macrocyclic core conformers

SUBMITTER: Stadelmann T 

PROVIDER: S-EPMC7796559 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature