Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation
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 wi...
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todo:paper_00039861_v622_n_p9_Bartesaghi2023-10-03T13:57:05Z Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation Bartesaghi, S. Herrera, D. Martinez, D.M. Petruk, A. Demicheli, V. Trujillo, M. Martí, M.A. Estrín, D.A. Radi, R. 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 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. Fil:Petruk, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrín, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v622_n_p9_Bartesaghi |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 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 |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Bartesaghi, S. Herrera, D. Martinez, D.M. Petruk, A. Demicheli, V. Trujillo, M. Martí, M.A. Estrín, D.A. Radi, R. |
| author_facet |
Bartesaghi, S. Herrera, D. Martinez, D.M. Petruk, A. Demicheli, V. Trujillo, M. Martí, M.A. Estrín, D.A. Radi, R. |
| author_sort |
Bartesaghi, S. |
| title |
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| title_short |
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| title_full |
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| title_fullStr |
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| title_full_unstemmed |
Tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| title_sort |
tyrosine oxidation and nitration in transmembrane peptides is connected to lipid peroxidation |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v622_n_p9_Bartesaghi |
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