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Oxidative Medicine and Cellular Longevity
Volume 2015, Article ID 319505, 22 pages
http://dx.doi.org/10.1155/2015/319505
Review Article

Nonenzymatic Reactions above Phospholipid Surfaces of Biological Membranes: Reactivity of Phospholipids and Their Oxidation Derivatives

1Institut d’Investigació en Ciències de la Salut (IUNICS), Departament de Química, Universitat de les Illes Balears, 07122 Palma de Mallorca, Spain
2Instituto de Investigación Sanitaria de Palma, 07010 Palma, Spain

Received 16 December 2014; Revised 24 March 2015; Accepted 25 March 2015

Academic Editor: Luciano Pirola

Copyright © 2015 Christian Solís-Calero et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. Y.-Y. Jiang, D.-X. Kong, T. Qin, X. Li, G. Caetano-Anollés, and H.-Y. Zhang, “The impact of oxygen on metabolic evolution: a chemoinformatic investigation,” PLoS Computational Biology, vol. 8, no. 3, Article ID e1002426, 2012. View at Publisher · View at Google Scholar · View at Scopus
  2. A. J. García-Sáez and P. Schwille, “Surface analysis of membrane dynamics,” Biochimica et Biophysica Acta—Biomembranes, vol. 1798, no. 4, pp. 766–776, 2010. View at Publisher · View at Google Scholar · View at Scopus
  3. E. Wallin and G. von Heijne, “Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms,” Protein Science, vol. 7, no. 4, pp. 1029–1038, 1998. View at Google Scholar · View at Scopus
  4. M. Pasenkiewicz-Gierula, K. Murzyn, T. Róg, and C. Czaplewski, “Molecular dynamics simulation studies of lipid bilayer systems,” Acta Biochimica Polonica, vol. 47, no. 3, pp. 601–611, 2000. View at Google Scholar · View at Scopus
  5. W. Dowhan, “The role of phospholipids in cell function,” Advances in Lipobiology, vol. 2, pp. 79–107, 1997. View at Publisher · View at Google Scholar · View at Scopus
  6. C. R. Sanders and K. F. Mittendorf, “Tolerance to changes in membrane lipid composition as a selected trait of membrane proteins,” Biochemistry, vol. 50, no. 37, pp. 7858–7867, 2011. View at Publisher · View at Google Scholar · View at Scopus
  7. A. Naudí, M. Jové, V. Ayala, R. Cabré, M. Portero-Otín, and R. Pamplona, “Non-enzymatic modification of aminophospholipids by carbonyl-amine reactions,” International Journal of Molecular Sciences, vol. 14, no. 2, pp. 3285–3313, 2013. View at Publisher · View at Google Scholar · View at Scopus
  8. G. van Meer, D. R. Voelker, and G. W. Feigenson, “Membrane lipids: where they are and how they behave,” Nature Reviews Molecular Cell Biology, vol. 9, no. 2, pp. 112–124, 2008. View at Publisher · View at Google Scholar · View at Scopus
  9. P. A. Janmey and P. K. J. Kinnunen, “Biophysical properties of lipids and dynamic membranes,” Trends in Cell Biology, vol. 16, no. 10, pp. 538–546, 2006. View at Publisher · View at Google Scholar · View at Scopus
  10. G. J. Bartlett, N. Borkakoti, and J. M. Thornton, “Catalysing new reactions during evolution: economy of residues and mechanism,” Journal of Molecular Biology, vol. 331, no. 4, pp. 829–860, 2003. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Y. Galperin and E. V. Koonin, “Divergence and convergence in enzyme evolution,” The Journal of Biological Chemistry, vol. 287, no. 1, pp. 21–28, 2012. View at Publisher · View at Google Scholar · View at Scopus
  12. K.-F. Wei, L.-J. Wu, J. Chen, Y.-F. Chen, and D.-X. Xie, “Structural evolution and functional diversification analyses of argonaute protein,” Journal of Cellular Biochemistry, vol. 113, no. 8, pp. 2576–2585, 2012. View at Publisher · View at Google Scholar · View at Scopus
  13. D. E. Almonacid and P. C. Babbitt, “Toward mechanistic classification of enzyme functions,” Current Opinion in Chemical Biology, vol. 15, no. 3, pp. 435–442, 2011. View at Publisher · View at Google Scholar · View at Scopus
  14. N. Lehman, “RNA in evolution,” Wiley Interdisciplinary Reviews: RNA, vol. 1, no. 2, pp. 202–213, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. T. Lan and Y. Lu, “Metal ion-dependent DNAzymes and their applications as biosensors,” Metal Ions in Life Sciences, vol. 10, pp. 217–248, 2012. View at Publisher · View at Google Scholar · View at Scopus
  16. W. Pan and G. A. Clawson, “Catalytic DNAzymes: derivations and functions,” Expert Opinion on Biological Therapy, vol. 8, no. 8, pp. 1071–1085, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. R. H. Michell, “Evolution of the diverse biological roles of inositols,” Biochemical Society Symposia, vol. 74, pp. 223–246, 2007. View at Publisher · View at Google Scholar · View at Scopus
  18. R. H. Michell, “Inositol derivatives: evolution and functions,” Nature Reviews Molecular Cell Biology, vol. 9, no. 2, pp. 151–161, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. C. Solís-Calero, J. Ortega-Castro, A. Hernández-Laguna, and F. Muñoz, “A comparative DFT study of the Schiff base formation from acetaldehyde and butylamine, glycine and phosphatidylethanolamine,” Theoretical Chemistry Accounts, vol. 131, no. 9, pp. 1263–1275, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. C. Solís-Calero, J. Ortega-Castro, and F. Muñoz, “DFT study on amino-phospholipids surface-mediated decomposition of hydrogen peroxide,” Journal of Physical Chemistry C, vol. 115, no. 46, pp. 22945–22953, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Yoshimoto, Y. Miyazaki, A. Umemoto, P. Walde, R. Kuboi, and K. Nakao, “Phosphatidylcholine vesicle-mediated decomposition of hydrogen peroxide,” Langmuir, vol. 23, no. 18, pp. 9416–9422, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. C. Solís-Calero, J. Ortega-Castro, A. Hernández-Laguna, and F. Muñoz, “A DFT study of the Amadori rearrangement above a phosphatidylethanolamine surface: comparison to reactions in aqueous environment,” The Journal of Physical Chemistry C, vol. 117, no. 16, pp. 8299–8309, 2013. View at Publisher · View at Google Scholar · View at Scopus
  23. C. Solís-Calero, J. Ortega-Castro, A. Hernández-Laguna, J. Frau, and F. Muñoz, “A DFT study of the carboxymethyl-phosphatidylethanolamine formation from glyoxal and phosphatidylethanolamine surface. Comparison with the formation of N(ε)-(carboxymethyl)lysine from glyoxal and L-lysine,” Physical Chemistry Chemical Physics, vol. 17, no. 12, pp. 8210–8222, 2015. View at Publisher · View at Google Scholar
  24. C. Solís-Calero, J. Ortega-Castro, A. Hernández-Laguna, and F. Muñoz, “DFT study of the mechanism of the reaction of aminoguanidine with methylglyoxal,” Journal of Molecular Modeling, vol. 20, no. 4, article 2202, 2014. View at Publisher · View at Google Scholar · View at Scopus
  25. R. M. Cordeiro, “Reactive oxygen species at phospholipid bilayers: distribution, mobility and permeation,” Biochimica et Biophysica Acta, vol. 1838, no. 1, pp. 438–444, 2014. View at Publisher · View at Google Scholar · View at Scopus
  26. H. Khandelia, B. Loubet, A. Olzyńska, P. Jurkiewicz, and M. Hof, “Pairing of cholesterol with oxidized phospholipid species in lipid bilayers,” Soft Matter, vol. 10, no. 4, pp. 639–647, 2014. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Štefl, R. Šachl, A. Olzyńska et al., “Comprehensive portrait of cholesterol containing oxidized membrane,” Biochimica et Biophysica Acta: Biomembranes, vol. 1838, no. 7, pp. 1769–1776, 2014. View at Publisher · View at Google Scholar · View at Scopus
  28. E. Conte, F. M. Megli, H. Khandelia, G. Jeschke, and E. Bordignon, “Lipid peroxidation and water penetration in lipid bilayers: a W-band EPR study,” Biochimica et Biophysica Acta—Biomembranes, vol. 1828, no. 2, pp. 510–517, 2013. View at Publisher · View at Google Scholar · View at Scopus
  29. H. Khandelia and O. G. Mouritsen, “Lipid gymnastics: evidence of complete acyl chain reversal in oxidized phospholipids from molecular simulations,” Biophysical Journal, vol. 96, no. 7, pp. 2734–2743, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. P. T. Vernier, Z. A. Levine, Y.-H. Wu et al., “Electroporating fields target oxidatively damaged areas in the cell membrane,” PLoS ONE, vol. 4, no. 11, Article ID e7966, 2009. View at Publisher · View at Google Scholar · View at Scopus
  31. J. Wong-Ekkabut, Z. Xu, W. Triampo, I.-M. Tang, D. P. Tieleman, and L. Monticelli, “Effect of lipid peroxidation on the properties of lipid bilayers: a molecular dynamics study,” Biophysical Journal, vol. 93, no. 12, pp. 4225–4236, 2007. View at Publisher · View at Google Scholar · View at Scopus
  32. S. Pogodin and V. A. Baulin, “Coarse-grained models of phospholipid membranes within the single chain mean field theory,” Soft Matter, vol. 6, no. 10, pp. 2216–2226, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. M. L. Berkowitz, “Detailed molecular dynamics simulations of model biological membranes containing cholesterol,” Biochimica et Biophysica Acta, vol. 1788, no. 1, pp. 86–96, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. A. K. Sum, R. Faller, and J. J. de Pablo, “Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides,” Biophysical Journal, vol. 85, no. 5, pp. 2830–2844, 2003. View at Publisher · View at Google Scholar · View at Scopus
  35. H. L. Scott, “Modeling the lipid component of membranes,” Current Opinion in Structural Biology, vol. 12, no. 4, pp. 495–502, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. K. Sugimori, H. Kawabe, H. Nagao, and K. Nishikawa, “Ab initio and DFT study of 31P-NMR chemical shifts of sphingomyelin and dihydrosphingomyelin lipid molecule,” International Journal of Quantum Chemistry, vol. 109, no. 15, pp. 3685–3693, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. S. Krishnamurty, M. Stefanov, T. Mineva et al., “Density functional theory-based conformational analysis of a phospholipid molecule (dimyristoyl phosphatidylcholine),” Journal of Physical Chemistry B, vol. 112, no. 42, pp. 13433–13442, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. J. A. Snyder and J. D. Madura, “Interaction of the phospholipid head group with representative quartz and aluminosilicate structures: an Ab initio study,” Journal of Physical Chemistry B, vol. 112, no. 23, pp. 7095–7103, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. N. C. Hernández and J. F. Sanz, “From periodic DFT calculations to classical molecular dynamics simulations,” Computational Materials Science, vol. 35, no. 3, pp. 183–186, 2006. View at Publisher · View at Google Scholar · View at Scopus
  40. G. Makov and M. C. Payne, “Periodic boundary conditions in ab initio calculations,” Physical Review B, vol. 51, no. 7, pp. 4014–4022, 1995. View at Publisher · View at Google Scholar · View at Scopus
  41. S. Franzen, “Use of periodic boundary conditions to calculate accurate β-sheet frequencies using density functional theory,” Journal of Physical Chemistry A, vol. 107, no. 46, pp. 9898–9902, 2003. View at Publisher · View at Google Scholar · View at Scopus
  42. J. Weng and W. Wang, “Molecular dynamics simulation of membrane proteins,” Advances in Experimental Medicine and Biology, vol. 805, pp. 305–329, 2014. View at Publisher · View at Google Scholar · View at Scopus
  43. D. P. Tieleman, S. J. Marrink, and H. J. C. Berendsen, “A computer perspective of membranes: molecular dynamics studies of lipid bilayer systems,” Biochimica et Biophysica Acta—Reviews on Biomembranes, vol. 1331, no. 3, pp. 235–270, 1997. View at Publisher · View at Google Scholar · View at Scopus
  44. P. Jurkiewicz, A. Olzyńska, L. Cwiklik et al., “Biophysics of lipid bilayers containing oxidatively modified phospholipids: insights from fluorescence and EPR experiments and from MD simulations,” Biochimica et Biophysica Acta—Biomembranes, vol. 1818, no. 10, pp. 2388–2402, 2012. View at Publisher · View at Google Scholar · View at Scopus
  45. J. F. Nagle and S. Tristram-Nagle, “Structure of lipid bilayers,” Biochimica et Biophysica Acta—Reviews on Biomembranes, vol. 1469, no. 3, pp. 159–195, 2000. View at Publisher · View at Google Scholar · View at Scopus
  46. S. V. Bennun, M. I. Hoopes, C. Xing, and R. Faller, “Coarse-grained modeling of lipids,” Chemistry and Physics of Lipids, vol. 159, no. 2, pp. 59–66, 2009. View at Publisher · View at Google Scholar · View at Scopus
  47. S. J. Marrink, H. J. Risselada, S. Yefimov, D. P. Tieleman, and A. H. De Vries, “The MARTINI force field: coarse grained model for biomolecular simulations,” The Journal of Physical Chemistry B, vol. 111, no. 27, pp. 7812–7824, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. M. G. Saunders and G. A. Voth, “Coarse-graining methods for computational biology,” Annual Review of Biophysics, vol. 42, no. 1, pp. 73–93, 2013. View at Publisher · View at Google Scholar · View at Scopus
  49. S. J. Singer and G. L. Nicolson, “The fluid mosaic model of the structure of cell membranes,” Science, vol. 175, no. 4023, pp. 720–731, 1972. View at Publisher · View at Google Scholar · View at Scopus
  50. M. Langner and K. Kubica, “The electrostatics of lipid surfaces,” Chemistry and Physics of Lipids, vol. 101, no. 1, pp. 3–35, 1999. View at Publisher · View at Google Scholar · View at Scopus
  51. M. Subramanian, A. Jutila, and P. K. J. Kinnunen, “Binding and dissociation of cytochrome c to and from membranes containing acidic phospholipids,” Biochemistry, vol. 37, no. 5, pp. 1394–1402, 1998. View at Publisher · View at Google Scholar · View at Scopus
  52. A. Toker and L. C. Cantley, “Signalling through the lipid products of phosphoinositide-3-OH kinase,” Nature, vol. 387, no. 6634, pp. 673–676, 1997. View at Publisher · View at Google Scholar · View at Scopus
  53. H. Brockman, “Dipole potential of lipid membranes,” Chemistry and Physics of Lipids, vol. 73, no. 1-2, pp. 57–79, 1994. View at Publisher · View at Google Scholar · View at Scopus
  54. G. Cevc, “Membrane electrostatics,” Biochimica et Biophysica Acta—Biomembranes, vol. 1031, no. 3, pp. 311–382, 1990. View at Publisher · View at Google Scholar · View at Scopus
  55. M. C. Wiener and S. H. White, “Fluid bilayer structure determination by the combined use of X-ray and neutron diffraction. I. Fluid bilayer models and the limits of resolution,” Biophysical Journal, vol. 59, no. 1, pp. 162–173, 1991. View at Publisher · View at Google Scholar · View at Scopus
  56. M. C. Wiener and S. H. White, “Fluid bilayer structure determination by the combined use of X-ray and neutron diffraction. II. ‘Composition-space’ refinement method,” Biophysical Journal, vol. 59, no. 1, pp. 174–185, 1991. View at Publisher · View at Google Scholar · View at Scopus
  57. S. H. White and M. C. Wiener, “Determination of the structure of fluid lipid bilayer membranes,” in Permeability and Stability of Lipid Bilayers, E. A. Disalvo and S. A. Simon, Eds., pp. 1–19, CRC Press, Boca Raton, Fla, USA, 1995. View at Google Scholar
  58. M. L. Belaya, M. V. Feigelman, and V. G. Levadny, “Hydration forces as a result of non-local water polarizability,” Chemical Physics Letters, vol. 126, no. 3-4, pp. 361–364, 1986. View at Publisher · View at Google Scholar · View at Scopus
  59. R. Kjellander and S. Marcelja, “Polarisation of water between molecular surfaces: a molecular dynamics study,” Chemica Scripta, vol. 25, pp. 73–80, 1985. View at Google Scholar
  60. R. Kjellander and S. Marčelja, “Perturbation of hydrogen bonding in water near polar surfaces,” Chemical Physics Letters, vol. 120, no. 4-5, pp. 393–396, 1985. View at Publisher · View at Google Scholar · View at Scopus
  61. A. Debnath, B. Mukherjee, K. G. Ayappa, P. K. Maiti, and S.-T. Lin, “Entropy and dynamics of water in hydration layers of a bilayer,” The Journal of Chemical Physics, vol. 133, no. 17, Article ID 174704, 2010. View at Publisher · View at Google Scholar · View at Scopus
  62. V. Lukacova, M. Peng, R. Tandlich, A. Hinderliter, and S. Balaz, “Partitioning of organic compounds in phases imitating the headgroup and core regions of phospholipid bilayers,” Langmuir, vol. 22, no. 4, pp. 1869–1874, 2006. View at Publisher · View at Google Scholar · View at Scopus
  63. I. Tsogas, D. Tsiourvas, G. Nounesis, and C. M. Paleos, “Interaction of poly-L-arginine with dihexadecyl phosphate/phosphatidylcholine liposomes,” Langmuir, vol. 21, no. 13, pp. 5997–6001, 2005. View at Publisher · View at Google Scholar · View at Scopus
  64. J. A. Barry and K. Gawrisch, “Direct NMR evidence for ethanol binding to the lipid-water interface of phospholipid bilayers,” Biochemistry, vol. 33, no. 26, pp. 8082–8088, 1994. View at Publisher · View at Google Scholar · View at Scopus
  65. A. Ortiz, F. J. Aranda, and J. A. Teruel, “Interaction of dirhamnolipid biosurfactants with phospholipid membranes: a molecular level study,” Advances in Experimental Medicine and Biology, vol. 672, pp. 42–53, 2010. View at Publisher · View at Google Scholar · View at Scopus
  66. G. Da Costa, L. Mouret, S. Chevance, E. Le Rumeur, and A. Bondon, “NMR of molecules interacting with lipids in small unilamellar vesicles,” European Biophysics Journal, vol. 36, no. 8, pp. 933–942, 2007. View at Publisher · View at Google Scholar · View at Scopus
  67. E. J. Prenner, R. N. A. H. Lewis, and R. N. McElhaney, “The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes,” Biochimica et Biophysica Acta—Biomembranes, vol. 1462, no. 1-2, pp. 201–221, 1999. View at Publisher · View at Google Scholar · View at Scopus
  68. A. Y. Mulkidjanian, J. Heberle, and D. A. Cherepanov, “Protons @ interfaces: implications for biological energy conversion,” Biochimica et Biophysica Acta: Bioenergetics, vol. 1757, no. 8, pp. 913–930, 2006. View at Publisher · View at Google Scholar · View at Scopus
  69. M. Haro, B. Giner, C. Lafuente, M. C. López, F. M. Royo, and P. Cea, “Proton sponge and fatty acid interactions at the air-water interface. Thermodynamic, spectroscopic, and microscopic study,” Langmuir, vol. 21, no. 7, pp. 2796–2803, 2005. View at Publisher · View at Google Scholar · View at Scopus
  70. P. Ädelroth and P. Brzezinski, “Surface-mediated proton-transfer reactions in membrane-bound proteins,” Biochimica et Biophysica Acta—Bioenergetics, vol. 1655, no. 1–3, pp. 102–115, 2004. View at Publisher · View at Google Scholar · View at Scopus
  71. G. L. Squadrito, E. M. Postlethwait, and S. Matalon, “Elucidating mechanisms of chlorine toxicity: reaction kinetics, thermodynamics, and physiological implications,” American Journal of Physiology—Lung Cellular and Molecular Physiology, vol. 299, no. 3, pp. L289–L300, 2010. View at Publisher · View at Google Scholar · View at Scopus
  72. R. Zamora and F. J. Hidalgo, “Phosphatidylethanolamine modification by oxidative stress product 4,5(E)-epoxy-2(E)-heptenal,” Chemical Research in Toxicology, vol. 16, no. 12, pp. 1632–1641, 2003. View at Publisher · View at Google Scholar · View at Scopus
  73. B. Vilanova, J. M. Gallardo, C. Caldés et al., “Formation of Schiff bases of O-phosphorylethanolamine and O-phospho-d, l-serine with pyridoxal 5-phosphate. Experimental and theoretical studies,” Journal of Physical Chemistry A, vol. 116, no. 8, pp. 1897–1905, 2012. View at Publisher · View at Google Scholar · View at Scopus
  74. C. Caldés, B. Vilanova, M. Adrover, F. Muñoz, and J. Donoso, “Understanding non-enzymatic aminophospholipid glycation and its inhibition. Polar head features affect the kinetics of Schiff base formation,” Bioorganic and Medicinal Chemistry, vol. 19, no. 15, pp. 4536–4543, 2011. View at Publisher · View at Google Scholar · View at Scopus
  75. E. Wachtel, D. Bach, R. F. Epand, A. Tishbee, and R. M. Epand, “A product of ozonolysis of cholesterol alters the biophysical properties of phosphatidylethanolamine membranes,” Biochemistry, vol. 45, no. 4, pp. 1345–1351, 2006. View at Publisher · View at Google Scholar · View at Scopus
  76. M. Yoshimoto, Y. Miyazaki, M. Sato, K. Fukunaga, R. Kuboi, and K. Nakao, “Mechanism for high stability of liposomal glucose oxidase to inhibitor hydrogen peroxide produced in prolonged glucose oxidation,” Bioconjugate Chemistry, vol. 15, no. 5, pp. 1055–1061, 2004. View at Publisher · View at Google Scholar · View at Scopus
  77. C. Solís-Calero, J. Ortega-Castro, and F. Muñoz, “Reactivity of a phospholipid monolayer model under periodic boundary conditions: a density functional theory study of the schiff base formation between phosphatidylethanolamine and acetaldehyde,” Journal of Physical Chemistry B, vol. 114, no. 48, pp. 15879–15885, 2010. View at Publisher · View at Google Scholar · View at Scopus
  78. E. Schnitzer, I. Pinchuk, and D. Lichtenberg, “Peroxidation of liposomal lipids,” European Biophysics Journal, vol. 36, no. 4-5, pp. 499–515, 2007. View at Publisher · View at Google Scholar · View at Scopus
  79. A. M. Bouchet, M. A. Frías, F. Lairion et al., “Structural and dynamical surface properties of phosphatidylethanolamine containing membranes,” Biochimica et Biophysica Acta, vol. 1788, no. 5, pp. 918–925, 2009. View at Publisher · View at Google Scholar · View at Scopus
  80. M. Rao, J. Eichberg, and J. Oró, “Synthesis of phosphatidylethanolamine under possible primitive earth conditions,” Journal of Molecular Evolution, vol. 25, no. 1, pp. 1–6, 1987. View at Publisher · View at Google Scholar · View at Scopus
  81. E. Hokazono, H. Tamezane, T. Hotta, Y. Kayamori, and S. Osawa, “Enzymatic assay of phosphatidylethanolamine in serum using amine oxidase from Arthrobacter sp,” Clinica Chimica Acta, vol. 412, no. 15-16, pp. 1436–1440, 2011. View at Publisher · View at Google Scholar · View at Scopus
  82. Y. Zhang, X. Wang, Z. Xiang et al., “Promotion of cellular migration and apoptosis resistance by a mouse eye-specific phosphatidylethanolamine-binding protein,” International Journal of Molecular Medicine, vol. 19, no. 1, pp. 55–63, 2007. View at Google Scholar · View at Scopus
  83. L. A. Falls, B. Furie, and B. C. Furie, “Role of phosphatidylethanolamine in assembly and function of the factor IXa—factor VIIIa complex on membrane surfaces,” Biochemistry, vol. 39, no. 43, pp. 13216–13222, 2000. View at Publisher · View at Google Scholar · View at Scopus
  84. A. Signorell, J. Jelk, M. Rauch, and P. Bütikofer, “Phosphatidylethanolamine is the precursor of the ethanolamine phosphoglycerol moiety bound to eukaryotic elongation factor 1A,” The Journal of Biological Chemistry, vol. 283, no. 29, pp. 20320–20329, 2008. View at Publisher · View at Google Scholar · View at Scopus
  85. A. K. Menon and V. L. Stevens, “Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein,” The Journal of Biological Chemistry, vol. 267, no. 22, pp. 15277–15280, 1992. View at Google Scholar · View at Scopus
  86. O. Higuchi, K. Nakagawa, T. Tsuzuki, T. Suzuki, S. Oikawa, and T. Miyazawa, “Aminophospholipid glycation and its inhibitor screening system: a new role of pyridoxal 5′-phosphate as the inhibitor,” Journal of Lipid Research, vol. 47, no. 5, pp. 964–974, 2006. View at Publisher · View at Google Scholar · View at Scopus
  87. A. Mulgrew-Nesbitt, K. Diraviyam, J. Wang et al., “The role of electrostatics in protein-membrane interactions,” Biochimica et Biophysica Acta—Molecular and Cell Biology of Lipids, vol. 1761, no. 8, pp. 812–826, 2006. View at Publisher · View at Google Scholar · View at Scopus
  88. A. Zachowski, “Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement,” Biochemical Journal, vol. 294, no. 1, pp. 1–14, 1993. View at Google Scholar · View at Scopus
  89. K. Asano, M. Miwa, K. Miwa et al., “Masking of phosphatidylserine inhibits apoptotic cell engulfment and induces autoantibody production in mice,” The Journal of Experimental Medicine, vol. 200, no. 4, pp. 459–467, 2004. View at Publisher · View at Google Scholar · View at Scopus
  90. B. Verhoven, R. A. Schlegel, and P. Williamson, “Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes,” Journal of Experimental Medicine, vol. 182, no. 5, pp. 1597–1601, 1995. View at Publisher · View at Google Scholar · View at Scopus
  91. E. Maciel, R. N. Da Silva, C. Simões et al., “Liquid chromatography-tandem mass spectrometry of phosphatidylserine advanced glycated end products,” Chemistry and Physics of Lipids, vol. 174, pp. 1–7, 2013. View at Publisher · View at Google Scholar · View at Scopus
  92. Y. Wang, W. Beck, R. Deppisch, S. M. Marshall, N. A. Hoenich, and M. G. Thompson, “Advanced glycation end products elicit externalization of phosphatidylserine in a subpopulation of platelets via 5-HT2A/2C receptors,” American Journal of Physiology—Cell Physiology, vol. 293, no. 1, pp. C328–C336, 2007. View at Publisher · View at Google Scholar · View at Scopus
  93. J. E. Vance and G. Tasseva, “Formation and function of phosphatidylserine and phosphatidylethanolamine in mammalian cells,” Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids, vol. 1831, no. 3, pp. 543–554, 2013. View at Publisher · View at Google Scholar · View at Scopus
  94. T. Yeung, G. E. Gilbert, J. Shi, J. Silvius, A. Kapus, and S. Grinstein, “Membrane phosphatidylserine regulates surface charge and protein localization,” Science, vol. 319, no. 5860, pp. 210–213, 2008. View at Publisher · View at Google Scholar · View at Scopus
  95. T. Yeung, B. Heit, J.-F. Dubuisson et al., “Contribution of phosphatidylserine to membrane surface charge and protein targeting during phagosome maturation,” The Journal of Cell Biology, vol. 185, no. 5, pp. 917–928, 2009. View at Publisher · View at Google Scholar · View at Scopus
  96. C. T. Sigal, W. Zhou, C. A. Buser, S. McLaughlin, and M. D. Resh, “Amino-terminal basic residues of Src mediate membrane binding through electrostatic interaction with acidic phospholipids,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 25, pp. 12253–12257, 1994. View at Publisher · View at Google Scholar · View at Scopus
  97. Z. Li, L. B. Agellon, and D. E. Vance, “Phosphatidylcholine homeostasis and liver failure,” The Journal of Biological Chemistry, vol. 280, no. 45, pp. 37798–37802, 2005. View at Publisher · View at Google Scholar · View at Scopus
  98. K. V. Damodaran, K. M. Merz Jr., and B. P. Gaber, “Structure and dynamics of the dilauroylphosphatidylethanolamine lipid bilayer,” Biochemistry®, vol. 31, no. 33, pp. 7656–7664, 1992. View at Publisher · View at Google Scholar · View at Scopus
  99. K. V. Damodaran and K. M. Merz Jr., “A comparison of DMPC- and DLPE-based lipid bilayers,” Biophysical Journal, vol. 66, no. 4, pp. 1076–1087, 1994. View at Publisher · View at Google Scholar · View at Scopus
  100. M. J. Dougherty and F. H. Arnold, “Directed evolution: new parts and optimized function,” Current Opinion in Biotechnology, vol. 20, no. 4, pp. 486–491, 2009. View at Publisher · View at Google Scholar · View at Scopus
  101. R. P. Richter, J. L. K. Him, and A. Brisson, “Supported lipid membranes,” Materials Today, vol. 6, no. 11, pp. 32–37, 2003. View at Publisher · View at Google Scholar · View at Scopus
  102. S. Biswas, N. S. Dodwadkar, P. P. Deshpande, and V. P. Torchilin, “Liposomes loaded with paclitaxel and modified with novel triphenylphosphonium-PEG-PE conjugate possess low toxicity, target mitochondria and demonstrate enhanced antitumor effects in vitro and in vivo,” Journal of Controlled Release, vol. 159, no. 3, pp. 393–402, 2012. View at Publisher · View at Google Scholar · View at Scopus
  103. M. Sánchez, F. J. Aranda, J. A. Teruel, and A. Ortiz, “New pH-sensitive liposomes containing phosphatidylethanolamine and a bacterial dirhamnolipid,” Chemistry and Physics of Lipids, vol. 164, no. 1, pp. 16–23, 2011. View at Publisher · View at Google Scholar · View at Scopus
  104. D. C. Drummond, M. Zignani, and J.-C. Leroux, “Current status of pH-sensitive liposomes in drug delivery,” Progress in Lipid Research, vol. 39, no. 5, pp. 409–460, 2000. View at Publisher · View at Google Scholar · View at Scopus
  105. H. Karanth and R. S. R. Murthy, “pH-sensitive liposomes—principle and application in cancer therapy,” Journal of Pharmacy and Pharmacology, vol. 59, no. 4, pp. 469–483, 2007. View at Publisher · View at Google Scholar · View at Scopus
  106. J. Wang, Y. Wang, and W. Liang, “Delivery of drugs to cell membranes by encapsulation in PEG-PE micelles,” Journal of Controlled Release, vol. 160, no. 3, pp. 637–651, 2012. View at Publisher · View at Google Scholar · View at Scopus
  107. R. R. Sawant and V. P. Torchilin, “Polymeric micelles: polyethylene glycol-phosphatidylethanolamine (PEG-PE)-based micelles as an example,” Methods in Molecular Biology, vol. 624, pp. 131–149, 2010. View at Publisher · View at Google Scholar · View at Scopus
  108. L. Mu, T. A. Elbayoumi, and V. P. Torchilin, “Mixed micelles made of poly(ethylene glycol)-phosphatidylethanolamine conjugate and D-α-tocopheryl polyethylene glycol 1000 succinate as pharmaceutical nanocarriers for camptothecin,” International Journal of Pharmaceutics, vol. 306, no. 1-2, pp. 142–149, 2005. View at Publisher · View at Google Scholar · View at Scopus
  109. B. Halliwell and J. Gutteridge, Free Radicals in Biology and Medicine, Oxford University Press, 4th edition, 2007.
  110. W. Dröge, “Free radicals in the physiological control of cell function,” Physiological Reviews, vol. 82, no. 1, pp. 47–95, 2002. View at Google Scholar · View at Scopus
  111. D. Ivanova, R. Bakalova, D. Lazarova, V. Gadjeva, and Z. Zhelev, “The impact of reactive oxygen species on anticancer therapeutic strategies,” Advances in Clinical and Experimental Medicine, vol. 22, no. 6, pp. 899–908, 2013. View at Google Scholar · View at Scopus
  112. A. Reis and C. M. Spickett, “Chemistry of phospholipid oxidation,” Biochimica et Biophysica Acta, vol. 1818, no. 10, pp. 2374–2387, 2012. View at Publisher · View at Google Scholar · View at Scopus
  113. R. Pamplona, “Advanced lipoxidation end-products,” Chemico-Biological Interactions, vol. 192, no. 1-2, pp. 14–20, 2011. View at Publisher · View at Google Scholar · View at Scopus
  114. R. Battino, T. R. Rettich, and T. Tominaga, “The solubility of oxygen and ozone in liquids,” Journal of Physical and Chemical Reference Data, vol. 12, no. 2, pp. 163–178, 1983. View at Publisher · View at Google Scholar
  115. X. Liu, M. J. S. Miller, M. S. Joshi, D. D. Thomas, and J. R. Lancaster Jr., “Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 5, pp. 2175–2179, 1998. View at Publisher · View at Google Scholar · View at Scopus
  116. E. Codorniu-Hernández and P. G. Kusalik, “Mobility mechanism of hydroxyl radicals in aqueous solution via hydrogen transfer,” Journal of the American Chemical Society, vol. 134, no. 1, pp. 532–538, 2012. View at Publisher · View at Google Scholar · View at Scopus
  117. A. Catalá, “An overview of lipid peroxidation with emphasis in outer segments of photoreceptors and the chemiluminescence assay,” The International Journal of Biochemistry and Cell Biology, vol. 38, no. 9, pp. 1482–1495, 2006. View at Publisher · View at Google Scholar · View at Scopus
  118. S. E. Norris, T. W. Mitchell, and P. L. Else, “Phospholipid peroxidation: lack of effect of fatty acid pairing,” Lipids, vol. 47, no. 5, pp. 451–460, 2012. View at Publisher · View at Google Scholar · View at Scopus
  119. A. Catalá, “Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids active in physiological and/or pathological conditions,” Chemistry and Physics of Lipids, vol. 157, no. 1, pp. 1–11, 2009. View at Publisher · View at Google Scholar · View at Scopus
  120. G. R. Buettner, “The pecking order of free radicals and antioxidants: lipid peroxidation, α-tocopherol, and ascorbate,” Archives of Biochemistry and Biophysics, vol. 300, no. 2, pp. 535–543, 1993. View at Publisher · View at Google Scholar · View at Scopus
  121. S. H. Lee, T. Oe, and I. A. Blair, “Vitamin C-induced decomposition of lipid hydroperoxides to endogenous genotoxins,” Science, vol. 292, no. 5524, pp. 2083–2086, 2001. View at Publisher · View at Google Scholar · View at Scopus
  122. A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre, “Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors,” British Journal of Pharmacology, vol. 153, no. 1, pp. 6–20, 2008. View at Publisher · View at Google Scholar · View at Scopus
  123. S. K. Jain, “The accumulation of malonyldialdehyde, a product of fatty acid peroxidation, can disturb aminophospholipid organization in the membrane bilayer of human erythrocytes,” The Journal of Biological Chemistry, vol. 259, no. 6, pp. 3391–3394, 1984. View at Google Scholar · View at Scopus
  124. J. A. Imlay, “Cellular defenses against superoxide and hydrogen peroxide,” Annual Review of Biochemistry, vol. 77, pp. 755–776, 2008. View at Publisher · View at Google Scholar · View at Scopus
  125. M. V. Avshalumov, D. G. MacGregor, L. M. Sehgal, and M. E. Rice, “The glial antioxidant network and neuronal ascorbate: protective yet permissive for H2O 2 signaling,” Neuron Glia Biology, vol. 1, no. 04, p. 365, 2004. View at Publisher · View at Google Scholar
  126. O. Baud, A. E. Greene, J. Li, H. Wang, J. J. Volpe, and P. A. Rosenberg, “Glutathione peroxidase-catalase cooperativity is required for resistance to hydrogen peroxide by mature rat oligodendrocytes,” The Journal of Neuroscience, vol. 24, no. 7, pp. 1531–1540, 2004. View at Publisher · View at Google Scholar · View at Scopus
  127. C. W. Olanow, “A rationale for monoamine oxidase inhibition as neuroprotective therapy for Parkinson's disease,” Movement Disorders, vol. 8, no. 1, pp. S1–S7, 1993. View at Publisher · View at Google Scholar · View at Scopus
  128. H. Sies, “Role of metabolic H2O2 generation: redox signaling and oxidative stress,” The Journal of Biological Chemistry, vol. 289, no. 13, pp. 8735–8741, 2014. View at Publisher · View at Google Scholar · View at Scopus
  129. H. J. Forman, “Reactive oxygen species and α,β-unsaturated aldehydes as second messengers in signal transduction,” Annals of the New York Academy of Sciences, vol. 1203, pp. 35–44, 2010. View at Publisher · View at Google Scholar · View at Scopus
  130. L. Domínguez, A. Sosa-Peinado, and W. Hansberg, “Catalase evolved to concentrate H2O2 at its active site,” Archives of Biochemistry and Biophysics, vol. 500, no. 1, pp. 82–91, 2010. View at Publisher · View at Google Scholar · View at Scopus
  131. G. Groeger, C. Quiney, and T. G. Cotter, “Hydrogen peroxide as a cell-survival signaling molecule,” Antioxidants and Redox Signaling, vol. 11, no. 11, pp. 2655–2671, 2009. View at Publisher · View at Google Scholar · View at Scopus
  132. E. A. Veal, A. M. Day, and B. A. Morgan, “Hydrogen peroxide sensing and signaling,” Molecular Cell, vol. 26, no. 1, pp. 1–14, 2007. View at Publisher · View at Google Scholar · View at Scopus
  133. H. M. Semchyshyn, “Reactive carbonyl species in vivo: generation and dual biological effects,” The Scientific World Journal, vol. 2014, Article ID 417842, 10 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  134. P. Zimniak, “Relationship of electrophilic stress to aging,” Free Radical Biology and Medicine, vol. 51, no. 6, pp. 1087–1105, 2011. View at Publisher · View at Google Scholar · View at Scopus
  135. R. J. Schaur, “Basic aspects of the biochemical reactivity of 4-hydroxynonenal,” Molecular Aspects of Medicine, vol. 24, no. 4-5, pp. 149–159, 2003. View at Publisher · View at Google Scholar · View at Scopus
  136. R. Pamplona, “Membrane phospholipids, lipoxidative damage and molecular integrity: a causal role in aging and longevity,” Biochimica et Biophysica Acta, vol. 1777, no. 10, pp. 1249–1262, 2008. View at Publisher · View at Google Scholar · View at Scopus
  137. M. Guichardant, N. Bernoud-Hubac, B. Chantegrel, C. Deshayes, and M. Lagarde, “Aldehydes from n-6 fatty acid peroxidation. Effects on aminophospholipids,” Prostaglandins Leukotrienes and Essential Fatty Acids, vol. 67, no. 2-3, pp. 147–149, 2002. View at Publisher · View at Google Scholar · View at Scopus
  138. M. Guichardant, P. Taibi-Tronche, L. B. Fay, and M. Lagarde, “Covalent modifications of aminophospholipids by 4-hydroxynonenal,” Free Radical Biology and Medicine, vol. 25, no. 9, pp. 1049–1056, 1998. View at Publisher · View at Google Scholar · View at Scopus
  139. G. Poli and R. J. Schaur, “4-Hydroxynonenal in the pathomechanisms of oxidative stress,” IUBMB Life, vol. 50, no. 4-5, pp. 315–321, 2000. View at Publisher · View at Google Scholar · View at Scopus
  140. N. Bernoud-Hubac, L. B. Fay, V. Armarnath et al., “Covalent binding of isoketals to ethanolamine phospholipids,” Free Radical Biology and Medicine, vol. 37, no. 10, pp. 1604–1611, 2004. View at Publisher · View at Google Scholar · View at Scopus
  141. G. Vistoli, D. De Maddis, A. Cipak, N. Zarkovic, M. Carini, and G. Aldini, “Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation,” Free Radical Research, vol. 47, no. 1, pp. 3–27, 2013. View at Publisher · View at Google Scholar · View at Scopus
  142. Y. Wang and C.-T. Ho, “Flavour chemistry of methylglyoxal and glyoxal,” Chemical Society Reviews, vol. 41, no. 11, pp. 4140–4149, 2012. View at Publisher · View at Google Scholar · View at Scopus
  143. Z. Turk, “Glycotoxines, carbonyl stress and relevance to diabetes and its complications,” Physiological Research, vol. 59, no. 2, pp. 147–156, 2010. View at Google Scholar · View at Scopus
  144. T. Miyazawa, K. Nakagawa, S. Shimasaki, and R. Nagai, “Lipid glycation and protein glycation in diabetes and atherosclerosis,” Amino Acids, vol. 42, no. 4, pp. 1163–1170, 2012. View at Publisher · View at Google Scholar · View at Scopus
  145. N. Shoji, K. Nakagawa, A. Asai et al., “LC-MS/MS analysis of carboxymethylated and carboxyethylated phosphatidylethanolamines in human erythrocytes and blood plasma,” Journal of Lipid Research, vol. 51, no. 8, pp. 2445–2453, 2010. View at Publisher · View at Google Scholar · View at Scopus
  146. R. Pamplona, J. R. Requena, M. Portero-Otín, J. Prat, S. R. Thorpe, and M. J. Bellmunt, “Carboxymethylated phosphatidylethanolamine in mitochondrial membranes of mammals. Evidence for intracellular lipid glycoxidation,” European Journal of Biochemistry, vol. 255, no. 3, pp. 685–689, 1998. View at Publisher · View at Google Scholar · View at Scopus
  147. J. R. Requena, M. U. Ahmed, C. W. Fountain et al., “Carboxymethylethanolamine, a biomarker of phospholipid modification during the Maillard reaction in vivo,” The Journal of Biological Chemistry, vol. 272, no. 28, pp. 17473–17479, 1997. View at Publisher · View at Google Scholar · View at Scopus
  148. R. Nagai, K. Ikeda, Y. Kawasaki et al., “Conversion of Amadori product of Maillard reaction to N(ε)-(carboxymethyl)lysine in alkaline condition,” FEBS Letters, vol. 425, no. 2, pp. 355–360, 1998. View at Publisher · View at Google Scholar · View at Scopus
  149. P. J. Thornalley, “Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems—role in ageing and disease,” Drug Metabolism and Drug Interactions, vol. 23, no. 1-2, pp. 125–150, 2008. View at Google Scholar · View at Scopus
  150. C. M. Utzmann and M. O. Lederer, “Identification and quantification of aminophospholipid-linked Maillard compounds in model systems and egg yolk products,” Journal of Agricultural and Food Chemistry, vol. 48, no. 4, pp. 1000–1008, 2000. View at Publisher · View at Google Scholar · View at Scopus
  151. M. O. Lederer and M. Baumann, “Formation of a phospholipid-linked pyrrolecarbaldehyde from model reactions of D-glucose and 3-deoxyglucosone with phosphatidyl ethanolamine,” Bioorganic and Medicinal Chemistry, vol. 8, no. 1, pp. 115–121, 2000. View at Publisher · View at Google Scholar · View at Scopus
  152. V. Levi, A. M. Villamil Giraldo, P. R. Castello, J. P. F. C. Rossi, and F. L. González Flecha, “Effects of phosphatidylethanolamine glycation on lipid-protein interactions and membrane protein thermal stability,” Biochemical Journal, vol. 416, no. 1, pp. 145–152, 2008. View at Publisher · View at Google Scholar · View at Scopus
  153. E. Doria, D. Buonocore, A. Focarelli, and F. Marzatico, “Relationship between human aging muscle and oxidative system pathway,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 830257, 13 pages, 2012. View at Publisher · View at Google Scholar · View at Scopus
  154. P. Voss and W. Siems, “Clinical oxidation parameters of aging,” Free Radical Research, vol. 40, no. 12, pp. 1339–1349, 2006. View at Publisher · View at Google Scholar · View at Scopus
  155. K. Nowotny, T. Jung, T. Grune, and A. Höhn, “Accumulation of modified proteins and aggregate formation in aging,” Experimental Gerontology, vol. 59, pp. 3–12, 2014. View at Google Scholar
  156. T. Grune and K. J. A. Davies, “The proteasomal system and HNE-modified proteins,” Molecular Aspects of Medicine, vol. 24, no. 4-5, pp. 195–204, 2003. View at Publisher · View at Google Scholar · View at Scopus
  157. B. H. Toyama and M. W. Hetzer, “Protein homeostasis: live long, won't prosper,” Nature Reviews Molecular Cell Biology, vol. 14, no. 1, pp. 55–61, 2013. View at Publisher · View at Google Scholar · View at Scopus
  158. E. Eden, N. Geva-Zatorsky, I. Issaeva et al., “Proteome half-life dynamics in living human cells,” Science, vol. 331, no. 6018, pp. 764–768, 2011. View at Publisher · View at Google Scholar · View at Scopus
  159. A. J. Hulbert, R. Pamplona, R. Buffenstein, and W. A. Buttemer, “Life and death: metabolic rate, membrane composition, and life span of animals,” Physiological Reviews, vol. 87, no. 4, pp. 1175–1213, 2007. View at Publisher · View at Google Scholar · View at Scopus
  160. R. F. Krause and K. C. Beamer, “Apparent turnover of subcellular phospholipids in the liver of control and vitamin A-deficient rats,” Journal of Nutrition, vol. 102, no. 11, pp. 1465–1469, 1972. View at Google Scholar · View at Scopus
  161. L. Freysz, R. Bieth, and P. Mandel, “Kinetics of the biosynthesis of phospholipids in neurons and glial cells isolated from rat brain cortex,” Journal of Neurochemistry, vol. 16, no. 10, pp. 1417–1424, 1969. View at Publisher · View at Google Scholar · View at Scopus
  162. J. C. DeMar Jr., K. Ma, J. M. Bell, and S. I. Rapoport, “Half-lives of docosahexaenoic acid in rat brain phospholipids are prolonged by 15 weeks of nutritional deprivation of n-3 polyunsaturated fatty acids,” Journal of Neurochemistry, vol. 91, no. 5, pp. 1125–1137, 2004. View at Publisher · View at Google Scholar · View at Scopus
  163. J. T.Green, Z. Liu, and R. P. Bazinet, “Brain phospholipid arachidonic acid half-lives are not altered following 15 weeks of N-3 polyunsaturated fatty acid adequate or deprived diet,” The Journal of Lipid Research, vol. 51, no. 3, pp. 535–543, 2010. View at Publisher · View at Google Scholar · View at Scopus
  164. C. Ott, K. Jacobs, E. Haucke, A. Navarrete Santos, T. Grune, and A. Simm, “Role of advanced glycation end products in cellular signaling,” Redox Biology, vol. 2, no. 1, pp. 411–429, 2014. View at Publisher · View at Google Scholar · View at Scopus
  165. V. M. Monnier, “Intervention against the Maillard reaction in vivo,” Archives of Biochemistry and Biophysics, vol. 419, no. 1, pp. 1–15, 2003. View at Publisher · View at Google Scholar · View at Scopus
  166. R. Singh, A. Barden, T. Mori, and L. Beilin, “Advanced glycation end-products: a review,” Diabetologia, vol. 44, no. 2, pp. 129–146, 2001. View at Publisher · View at Google Scholar · View at Scopus
  167. M. Namiki and T. Hayashi, “A new mechanism of the Maillard reaction involving sugar fragmentation and free radical formation,” ACS Symposium Series, vol. 215, pp. 21–46, 1983. View at Google Scholar
  168. S. P. Wolff and R. T. Dean, “Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes,” Biochemical Journal, vol. 245, no. 1, pp. 243–250, 1987. View at Google Scholar · View at Scopus
  169. R. Casasnovas, M. Adrover, J. Ortega-Castro, J. Frau, J. Donoso, and F. Muñoz, “C-H activation in pyridoxal-5′-phosphate Schiff bases: the role of the imine nitrogen. A combined experimental and computational study,” The Journal of Physical Chemistry B, vol. 116, no. 35, pp. 10665–10675, 2012. View at Publisher · View at Google Scholar · View at Scopus
  170. R. Casasnovas, J. Frau, J. Ortega-Castro, J. Donoso, and F. Muñoz, “C-H activation in pyridoxal-5′-phosphate and pyridoxamine-5′—phosphate schiff bases: effect of metal chelation. A computational study,” The Journal of Physical Chemistry B, vol. 117, no. 8, pp. 2339–2347, 2013. View at Publisher · View at Google Scholar · View at Scopus
  171. J. Ortega-Castro, M. Adrover, J. Frau, A. Salvà, J. Donoso, and F. Muñoz, “DFT studies on schiff base formation of vitamin B6 analogues. Reaction between a pyridoxamine-Analogue and carbonyl compounds,” The Journal of Physical Chemistry A, vol. 114, no. 13, pp. 4634–4640, 2010. View at Publisher · View at Google Scholar · View at Scopus
  172. A. Salvà, J. Donoso, J. Frau, and F. Muñoz, “DFT studies on schiff base formation of vitamin B6 analogues,” The Journal of Physical Chemistry A, vol. 107, no. 44, pp. 9409–9414, 2003. View at Publisher · View at Google Scholar · View at Scopus
  173. D. K. Hincha and M. Hagemann, “Stabilization of model membranes during drying by compatible solutes involved in the stress tolerance of plants and microorganisms,” Biochemical Journal, vol. 383, no. 2, pp. 277–283, 2004. View at Publisher · View at Google Scholar · View at Scopus
  174. M. Del C. Luzardo, F. Amalfa, A. M. Nuñez, S. Díaz, A. C. Biondi De Lopez, and E. A. Disalvo, “Effect of trehalose and sucrose on the hydration and dipole potential of lipid bilayers,” Biophysical Journal, vol. 78, no. 5, pp. 2452–2458, 2000. View at Publisher · View at Google Scholar · View at Scopus
  175. N. M. Tsvetkova, B. L. Phillips, L. M. Crowe, J. H. Crowe, and S. H. Risbud, “Effect of sugars on headgroup mobility in freeze-dried dipalmitoylphosphatidylcholine bilayers: solid-state 31P NMR and FTIR studies,” Biophysical Journal, vol. 75, no. 6, pp. 2947–2955, 1998. View at Publisher · View at Google Scholar · View at Scopus
  176. C. S. Pereira and P. H. Hünenberger, “Interaction of the sugars trehalose, maltose and glucose with a phospholipid bilayer: a comparative molecular dynamics study,” Journal of Physical Chemistry B, vol. 110, no. 31, pp. 15572–15581, 2006. View at Publisher · View at Google Scholar · View at Scopus
  177. R. Ramasamy, S. F. Yan, and A. M. Schmidt, “Receptor for AGE (RAGE): signaling mechanisms in the pathogenesis of diabetes and its complications,” Annals of the New York Academy of Sciences, vol. 1243, no. 1, pp. 88–102, 2011. View at Publisher · View at Google Scholar · View at Scopus
  178. A. E. N. Ferreira, A. M. J. Ponces Freire, and E. O. Voit, “A quantitative model of the generation of Nε-(carboxymethyl)lysine in the Maillard reaction between collagen and glucose,” Biochemical Journal, vol. 376, no. 1, pp. 109–121, 2003. View at Publisher · View at Google Scholar · View at Scopus
  179. N. M. J. Hanssen, L. Engelen, I. Ferreira et al., “Plasma levels of advanced glycation endproducts Nϵ-(carboxymethyl)lysine, Nϵ-(carboxyethyl)lysine, and pentosidine are not independently associated with cardiovascular disease in individuals with or without type 2 diabetes: The Hoorn and CODAM studies,” The Journal of Clinical Endocrinology and Metabolism, vol. 98, no. 8, pp. E1369–E1373, 2013. View at Publisher · View at Google Scholar · View at Scopus
  180. I. Roncero-Ramos, C. Delgado-Andrade, F. J. Tessier et al., “Metabolic transit of Nε-carboxymethyl-lysine after consumption of AGEs from bread crust,” Food & Function, vol. 4, no. 7, pp. 1032–1039, 2013. View at Publisher · View at Google Scholar · View at Scopus
  181. R. Nagai, K. Ikeda, T. Higashi et al., “Hydroxyl radical mediates N(ε)-(carboxymethyl)lysine formation from Amadori product,” Biochemical and Biophysical Research Communications, vol. 234, no. 1, pp. 167–172, 1997. View at Publisher · View at Google Scholar · View at Scopus
  182. M. U. Ahmed, S. R. Thorpe, and J. W. Baynes, “Identification of N(ε)-carboxymethyllysine as a degradation product of fructoselysine in glycated protein,” Journal of Biological Chemistry, vol. 261, no. 11, pp. 4889–4894, 1986. View at Google Scholar · View at Scopus
  183. Y. Al-Abed and R. Bucala, “Nε-carboxymethyllysine formation by direct addition of glyoxal to lysine during the Maillard reaction,” Bioorganic and Medicinal Chemistry Letters, vol. 5, no. 18, pp. 2161–2162, 1995. View at Publisher · View at Google Scholar · View at Scopus
  184. K. J. Wells-Knecht, D. V. Zyzak, J. E. Litchfield, S. R. Thorpe, and J. W. Baynes, “Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose,” Biochemistry, vol. 34, no. 11, pp. 3702–3709, 1995. View at Publisher · View at Google Scholar · View at Scopus
  185. M. A. Glomb and V. M. Monnier, “Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction,” The Journal of Biological Chemistry, vol. 270, no. 17, pp. 10017–10026, 1995. View at Publisher · View at Google Scholar · View at Scopus
  186. F. J. Hidalgo and R. Zamora, “Interplay between the Maillard reaction and lipid peroxidation in biochemical systems,” Annals of the New York Academy of Sciences, vol. 1043, pp. 319–326, 2005. View at Publisher · View at Google Scholar · View at Scopus