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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Lysozyme oxidation by singlet molecular oxygen: Peptide characterization using [O-18]-labeling oxygen and nLC-MS/MS

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Author(s):
Marques, Emerson Finco ; Medeiros, Marisa H. G. ; Di Mascio, Paolo [1]
Total Authors: 3
Affiliation:
[1] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508000 Sao Paulo, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: Journal of Mass Spectrometry; v. 52, n. 11, p. 739-751, NOV 2017.
Web of Science Citations: 3
Abstract

Singlet molecular oxygen (O-1(2)) is generated in biological systems and reacts with different biomolecules. Proteins are a major target for O-1(2), and His, Tyr, Met, Cys, and Trp are oxidized at physiological pH. In the present study, the modification of lysozyme protein by O-1(2) was investigated using mass spectrometry approaches. The experimental findings showed methionine, histidine, and tryptophan oxidation. The experiments were achieved using {[}O-18]-labeled O-1(2) released from thermolabile endoperoxides in association with nano-scale liquid chromatography coupled to electrospray ionization mass spectrometry. The structural characterization by nLC-MS/MS of the amino acids in the tryptic peptides of the proteins showed addition of {[}O-18]-labeling atoms in different amino acids. (AU)

FAPESP's process: 12/12663-1 - Singlet molecular oxygen and peroxides in chemical biology
Grantee:Paolo Di Mascio
Support type: Research Projects - Thematic Grants
FAPESP's process: 13/07937-8 - Redoxome - Redox Processes in Biomedicine
Grantee:Ohara Augusto
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC