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. 2022 Mar 21;37(1):912–929. doi: 10.1080/14756366.2022.2045590

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© 2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — MS/MS spectra of peptides modified by Ebselen. Representative MS/MS spectra for the 3 peptide sequences covalently modified by Ebselen (A) SIDGNLFCGFK (m/z = 738.2831, z = 2), (B) YQCVEFAR (m/z = 645.7306, z = 2) and (C) ELYLNCVR (m/z = 642.7532, z = 2). The Ebselen modification reporter ions (an intense signal of m/z = 275.9938 corresponding to protonated Ebselen ([Eb + H]⁺) and the signal of the two most intense fragmentation products of m/z = 196.0751 and 183.9417) are present in all spectra (Eb frag⁺). Peaks are assigned to the y and b series of native sequence; +Eb indicates those fragment ions containing the +274.985 modification. Phe, Lys and Tyr indicate the immoniun ions of the respective amino acids. Eb: Ebselen.