A Temperature-Driven, Reversible, Helical-Handedness Inversion in Peptaibol Analogues Tuned by the C-Terminal Capping Moiety

Marta De Zotti, Victoria N. Syryamina, Rohanah Hussain, Edoardo Longo, Giuliano Siligardi, Sergei A. Dzuba, Lorenzo Stella, Fernando Formaggio

Результат исследования: Научные публикации в периодических изданияхстатья

Аннотация

Trichogin is a natural peptide endowed with antimicrobial and antitumor activity. A member of the peptaibol family, trichogin possesses a C-terminal amino alcohol. In the past, this moiety was substituted for a methyl ester for synthetic purposes and it was observed that this apparently slight modification caused significant changes in the peptide bioactivity. With the aim of understanding the reasons behind such observations, a detailed spectroscopic study on a number of trichogin analogues has been performed. Herein, data obtained from synchrotron radiation circular dichroism, NMR spectroscopy, and fluorescence spectroscopy in organic solvents at cryogenic temperatures are compared with those independently acquired by means of EPR spectroscopy at 80 K. It is unambiguously revealed that the presence of a reversible, temperature-driven, screw-sense interconversion from a right- to left-handed helix is determined by the C-terminal capping moiety. Data demonstrate, for the first time, the key role of a C-terminal methyl ester in promoting peptide screw-sense inversion.

Язык оригиналаанглийский
Страницы (с-по)2125-2132
Число страниц8
ЖурналChemBioChem
Том20
Номер выпуска16
DOI
СостояниеОпубликовано - 16 авг 2019

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