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. 2015 Aug 5;10(8):e0130533. doi: 10.1371/journal.pone.0130533

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© 2015 Kiselar et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 1 — MALDI-TOF MS spectra obtained from native (untreated) rhBD-2 peptide (A) vs MGO-treated peptide (B). Native peptide exhibits singly and doubly protonated molecular ionic species at m/z 4326.6 and 2164.5, respectively. Exposure of rhBD-2 (20 ng/μl) to 100 μM MGO for 72 h resulted in additional peaks for both the singly and doubly protonated ionic species. Singly protonated ions (shaded area) show m/z increases of + 54 Da (m/z 4381.7), +72 Da (m/z 4399.7), and +126 Da (m/z 4453.7), suggesting adduction of dehydrated, intact, and dehydrated + intact MGO molecular species, respectively.