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Cyclic Peptoids as Mycotoxin Mimics: An Exploration of Their Structural and Biological Properties

2017; American Chemical Society; Volume: 82; Issue: 17 Linguagem: Inglês

10.1021/acs.joc.7b00965

1520-6904

Assunta D’Amato, Raffaele Volpe, Maria Carmela Vaccaro, Stefania Terracciano, Ines Bruno, Massimo Tosolini, Consiglia Tedesco, Giovanni Pierri, Paolo Tecilla, Chiara Costabile, Giorgio Della Sala, Irene Izzo, Francesco De Riccardis,

Microbial Natural Products and Biosynthesis

Cyclic peptoids have recently emerged as important examples of peptidomimetics for their interesting complexing properties and innate ability to permeate biological barriers. In the present contribution, experimental and theoretical data evidence the intricate conformational and stereochemical properties of five novel hexameric peptoids decorated with N-isopropyl, N-isobutyl, and N-benzyl substituents. Complexation studies by NMR, in the presence of sodium tetrakis[3,5-bis(trifluoromethyl)phenyl]borate (NaTFPB), theoretical calculations, and single-crystal X-ray analyses indicate that the conformationally stable host/guest metal adducts display architectural ordering comparable to that of the enniatins and beauvericin mycotoxins. Similarly to the natural depsipeptides, the synthetic oligolactam analogues show a correlation between ion transport abilities in artificial liposomes and cytotoxic activity on human cancer cell lines. The reported results demonstrate that the versatile cyclic peptoid scaffold, for its remarkable conformational and complexing properties, can morphologically mimic related natural products and elicit powerful biological activities.