Bartesaghi, S.; Herrera, D.; Martinez, D.M.; Petruk, A.; Demicheli, V.; Trujillo, M.; Martí, M.A.; Estrín, D.A.; Radi, R."Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation" (2017) Archives of Biochemistry and Biophysics. 622:9-25
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Tyrosine nitration is an oxidative post-translational modification that can occur in proteins associated to hydrophobic bio-structures such as membranes and lipoproteins. In this work, we have studied tyrosine nitration in membranes using a model system consisting of phosphatidylcholine liposomes with pre-incorporated tyrosine-containing 23 amino acid transmembrane peptides. Tyrosine residues were located at positions 4, 8 or 12 of the amino terminal, resulting in different depths in the bilayer. Tyrosine nitration was accomplished by exposure to peroxynitrite and a peroxyl radical donor or hemin in the presence of nitrite. In egg yolk phosphatidylcholine liposomes, nitration was highest for the peptide with tyrosine at position 8 and dramatically increased as a function of oxygen levels. Molecular dynamics studies support that the proximity of the tyrosine phenolic ring to the linoleic acid peroxyl radicals contributes to the efficiency of tyrosine oxidation. In turn, α-tocopherol inhibited both lipid peroxidation and tyrosine nitration. The mechanism of tyrosine nitration involves a “connecting reaction” by which lipid peroxyl radicals oxidize tyrosine to tyrosyl radical and was fully recapitulated by computer-assisted kinetic simulations. Altogether, this work underscores unique characteristics of the tyrosine oxidation and nitration process in lipid-rich milieu that is fueled via the lipid peroxidation process. © 2017 Elsevier Inc.


Documento: Artículo
Título:Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation
Autor:Bartesaghi, S.; Herrera, D.; Martinez, D.M.; Petruk, A.; Demicheli, V.; Trujillo, M.; Martí, M.A.; Estrín, D.A.; Radi, R.
Filiación:Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Avda. Gral. Flores 2125, Montevideo, 11800, Uruguay
Departamento de Educación Médica, Facultad de Medicina, Universidad de la República, Avda. Gral. Flores 2125, Montevideo, 11800, Uruguay
Center for Free Radical and Biomedical Research, Facultad de Medicina, Universidad de la República, Avda. Gral. Flores 2125, Montevideo, 11800, Uruguay
Departamento de Química Biológica and IQUIBICEN-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cuidad Universitaria, Pab 2, Buenos Aires, C1428EHA, Argentina
Departamento de Química Inorgánica, Analítica y Química-Física and INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Cuidad Universitaria, Pab 2, Buenos Aires, C1428EHA, Argentina
Palabras clave:Free radicals; Lipid peroxidation; Liposomes; Membranes; Peroxynitrite; Tyrosine nitration; 3 nitrotyrosine; alpha tocopherol; hemin; linoleic acid; lipid hydroperoxide; liposome; nitrite; oxygen; peptide; peroxy radical; peroxynitrite; phosphatidylcholine; transmembrane peptide; tyrosine; unclassified drug; unsaturated fatty acid; 2,2'-azobis(2-amidinopropane); amidine; free radical; peptide; peroxynitrous acid; tyrosine; amino terminal sequence; Article; bilayer membrane; comparative study; conformation; controlled study; kinetics; lipid composition; lipid peroxidation; liposome membrane; membrane model; molecular dynamics; nitration; oxidation; oxygen concentration; pH; priority journal; solvation; stoichiometry; amino acid sequence; cell membrane; chemistry; metabolism; oxidation reduction reaction; Amidines; Amino Acid Sequence; Cell Membrane; Free Radicals; Hemin; Lipid Peroxidation; Liposomes; Molecular Dynamics Simulation; Oxidation-Reduction; Oxygen; Peptides; Peroxynitrous Acid; Tyrosine
Página de inicio:9
Página de fin:25
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
CAS:3 nitrotyrosine, 3604-79-3; alpha tocopherol, 1406-18-4, 1406-70-8, 52225-20-4, 58-95-7, 59-02-9; hemin, 16009-13-5; linoleic acid, 1509-85-9, 2197-37-7, 60-33-3, 822-17-3; nitrite, 14797-65-0; oxygen, 7782-44-7; phosphatidylcholine, 55128-59-1, 8002-43-5; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; peroxynitrous acid, 14691-52-2; 2,2'-azobis(2-amidinopropane); Amidines; Free Radicals; Hemin; Liposomes; Oxygen; Peptides; Peroxynitrous Acid; Tyrosine


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---------- APA ----------
Bartesaghi, S., Herrera, D., Martinez, D.M., Petruk, A., Demicheli, V., Trujillo, M., Martí, M.A.,..., Radi, R. (2017) . Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation. Archives of Biochemistry and Biophysics, 622, 9-25.
---------- CHICAGO ----------
Bartesaghi, S., Herrera, D., Martinez, D.M., Petruk, A., Demicheli, V., Trujillo, M., et al. "Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation" . Archives of Biochemistry and Biophysics 622 (2017) : 9-25.
---------- MLA ----------
Bartesaghi, S., Herrera, D., Martinez, D.M., Petruk, A., Demicheli, V., Trujillo, M., et al. "Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation" . Archives of Biochemistry and Biophysics, vol. 622, 2017, pp. 9-25.
---------- VANCOUVER ----------
Bartesaghi, S., Herrera, D., Martinez, D.M., Petruk, A., Demicheli, V., Trujillo, M., et al. Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation. Arch. Biochem. Biophys. 2017;622:9-25.