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    Peptoids are attractive substitutes for peptides in several research areas, especially when they adopt a helical structure. The chain-size evolution of the secondary structure of the widely studied (S)-N-1-phenylethyl peptoids is here analyzed by means of the ion mobility mass spectrometry technique increasingly used as a powerful analytical tool and is further supported by theoretical modeling. We conclude that the helical shape of the peptoids prevailing in solution is lost in the gas phase by the need to screen the positive charge borne by the peptoid even though the collisional cross sections are close to the values expected for helical systems. We further illustrate that trend line analyses predicting molecular shapes from fits of the size evolution of cross sections can be very misleading since they critically depend on the range of polymerization degrees under study.


    Sébastien Hoyas, Emilie Halin, Vincent Lemaur, Julien De Winter, Pascal Gerbaux, Jérôme Cornil. Helicity of Peptoid Ions in the Gas Phase. Biomacromolecules. 2020 Feb 10;21(2):903-909

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    PMID: 31945292

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