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. 2020 Feb 4;21(3):1012. doi: 10.3390/ijms21031012

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Full-scan mass spectrometry (MS) and representative MS/MS spectra of QQPFP and its products (P1~P4) during plasma treatment, showing evidence for •OH-mediated modification. In each panel, the left spectrum shows the full scan, while the right spectrum shows the fragment ions. The b and y ions originated from preferential cleavage at the N-terminus and C-terminus of specific amino acid residues during collision-induced dissociation, respectively. (A) Original peptide (616.3 m/z); (B) product 1 (342.2 m/z); (C) product 2 (586.3 m/z); (D) product 3 (632.3 m/z); (E) product 4 (648.3 m/z).

Full-scan mass spectrometry (MS) and representative MS/MS spectra of QQPFP and its products (P1~P4) during plasma treatment, showing evidence for •OH-mediated modification. In each panel, the left spectrum shows the full scan, while the right spectrum shows the fragment ions. The b and y ions originated from preferential cleavage at the N-terminus and C-terminus of specific amino acid residues during collision-induced dissociation, respectively. (A) Original peptide (616.3 m/z); (B) product 1 (342.2 m/z); (C) product 2 (586.3 m/z); (D) product 3 (632.3 m/z); (E) product 4 (648.3 m/z).