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. 2019 Jul 24;10:931. doi: 10.3389/fphys.2019.00931

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Copyright © 2019 Kassa, Wood, Strader and Alayash.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Representative mass spectrometry data confirming the modification of HbS by TD-3, 5HMF, and HU. Intact mass (top-down) and LC/MS/MS (bottom-up) analysis were utilized to elucidate how the antisickling reagents interact with HbS. (A and B) Intact mass data confirm that TD-3 substantially modifies both β and α subunits. (C) Intact mass data confirms that 5HMF modifies both α and β subunits. (D) MS/MS fragmentation spectrum representing the y and b ions matched to the modified tryptic peptide GTFATSELHCDKLHVDPENFR (residues 83–104) from HbS incubated with HU. This peptide contains the diglycine signature modification (at βK96) associated with ubiquitination and S-nitrosylation (at βC93). The inset represents the extracted ion chromatogram representing the S-nitrosylated peptide.