A mono-proline analogue of the potent anthelmintic cyclooctadepsipeptide PF1022A has been synthesized. NMR studies in combination with molecular dynamics simulations demonstrate that the confirmation of this analogue is both rigidified and distorted compared with the asymmetric conformation of PF1022A. The backbone conformation is significant with respect to anthelmintic activity.
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Scherkenbeck et al. (1999) studied this question.
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