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. 2013 Aug 3;3(9):618–632. doi: 10.7150/thno.6810

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© Ivyspring International Publisher. This is an open-access article distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by-nc-nd/3.0/). Reproduction is permitted for personal, noncommercial use, provided that the article is in whole, unmodified, and properly cited.

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Fig 3 — Chemical stability of different macrocyclic Cu-complexes probed by MALDI-MS. MALDI-MS spectra are recorded under identical conditions for Cu-DOTA-AE105 in SA (panel A) and ACHA (panel B), Cu-CB-TE2A-AE105 in ACHA (panel C), and for Cu-CB-TE2A-PA-AE105 in ACHA (panel D). To the left of each panel is shown the best fit obtained for the isotope envelopes using the oxidation state of the bound Cu as the only floating parameter (Cu(II) or Cu(I)). The lower case letters in the MALDI-MS spectra indicates the monoisotopic peaks of the following singly charged molecular species: a) corresponds to the demetallated peptide, [M + H]⁺; b) corresponds to the Cu-chelated peptide with ⁶³Cu(II), [M - H + ⁶³Cu(II)]⁺.