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

Autor(es)

Marques, Emerson Finco ; Medeiros, Marisa H. G. ; Di Mascio, Paolo ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508000 Sao Paulo, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: Journal of Mass Spectrometry; v. 52, n. 11, p. 739-751, NOV 2017.
• Citações Web of Science: 2

Resumo

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)

• Processo FAPESP: 12/12663-1 - Oxigênio singlete e peróxidos em química biológica
• Beneficiário: Paolo Di Mascio
• Linha de fomento: Auxílio à Pesquisa - Temático
• Processo FAPESP: 13/07937-8 - Redoxoma
• Beneficiário: Ohara Augusto
• Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs