Comparative study on the conformation of phalloidin, viroisin, and related 
derivatives in aqueous solution

Kobayashi, Naohiro; Endo, Satoshi; Kobayashi, Hideyuki; Faulstich, Heinz; Wieland, Theodor; Munekata, Eisuke

doi:10.1111/j.1432-1033.1995.726zz.x

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Comparative study on the conformation of phalloidin, viroisin, and related derivatives in aqueous solution

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Faulstich, Heinz
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

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Wieland, Theodor
Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Kobayashi, N., Endo, S., Kobayashi, H., Faulstich, H., Wieland, T., & Munekata, E. (1995). Comparative study on the conformation of phalloidin, viroisin, and related derivatives in aqueous solution. European Journal of Biochemistry, 232(3), 726-736. doi:10.1111/j.1432-1033.1995.726zz.x.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-7480-5

Abstract

We investigated the conformations of toxic phalloidin and viroisin in aqueous solution using 500-MHz 1H-NMR spectroscopy in conjunction with molecular modeling. The conformations of two non-toxic phalloidin derivatives, secophalloidin and dethiophalloidin, were also correspondingly studied for comparison purposes. Results indicate that the non-toxic peptides have a multiple conformation, whereas the toxic peptides are comprised of a rigid molecule. It was found that the conformation of phalloidin partially resembles that of viroisin in the region of Cys3-Pro4-Ala5-Trp6, being different from that of the non-toxic peptides; thereby suggesting this region plays an important role leading to their toxicity.