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Structural Definition of Early Lysine and Histidine Adduction Chemistry of 4-Hydroxynonenal
Abstract
The lipid peroxidation product trans-4-hydroxy-2-nonenal (HNE) has been implicated in the covalent modification of low-density lipoproteins (LDL) thought to contribute to the over-accumulation of LDL in the arterial wall in the initial stages of atherosclerosis. Proposals for the exact structures of "early" protein side-chain modifications until now have been based on indirect evidence. In this paper, the structures of first-formed His- and Lys-based adducts were elucidated by correlating NMR spectral properties with those obtained on models with reduced chiral center content, in some cases following hydride reduction. In this manner, we could confirm unambiguously the structure of a HNE-His imidazole(N tau) Michael adduct, stabilized as a cyclic hemiacetal and isolated from a neutral aqueous 1:1 stoichiometry reaction mixture. In the case of Lys/amine reactivity, where an excess of amine is needed to avert HNE aldol condensation, the predominance of a 1:1 Michael adduct in homogeneous aqueous solution and a 1:2 Michael-Schiff base adduct under two-phase aqueous-organic conditions could be verified by isolation of the respective borohydride-reduced forms. The 1:2 adduct, shown to exist as the cyclic hemiaminal, could represent a stable lysine-based cross-link in certain protein microenvironments.
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Citations
Cited by
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Stadtman, E. R., & Berlett, B. S. (1998) · Drug Metabolism Reviews · doi:10.3109/03602539808996310 · Cited by 891
Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.815348 · Cited by 823
Catalá, A. (2009) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2008.09.004 · Cited by 745
Negre‐Salvayre, A., Coatrieux, C., Ingueneau, C., & Salvayre, R. (2008) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707395 · Cited by 641
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Singh, S., Brocker, C., Koppaka, V., Chen, Y., Jackson, B. C., Matsumoto, A., Thompson, D. C., & Vasiliou, V. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.11.010 · Cited by 601
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Gérard-Monnier, D., Erdelmeier, I., Régnard, K., Moze-Henry, N., Yadan, J.-C., & Chaudière, J. (1998) · Chemical Research in Toxicology · doi:10.1021/tx9701790 · Cited by 494
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Davies, M. J., & Truscott, R. J. W. (2001) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/s1011-1344(01)00208-1 · Cited by 448
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“5 in an equilibrium with their favored cyclic hemiacetal form [58].”
BackgroundOrigin and Mechanistic Pathways of Formation of the Parent FuranA Food Toxicant
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Subramaniam, R., Roediger, F., Jordan, B., Mattson, M. P., Keller, J. N., Waeg, G., & Butterfield, D. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031161.x · Cited by 270
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Lucas, D. T., & Szweda, L. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.510 · Cited by 254
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Metadata
- Authors
- Nadkarni, D. V., & Sayre, L. M.
- Venue
- Chemical Research in Toxicology
- Publisher
- American Chemical Society (ACS)
- Published
- 1995-03
- Volume
- 8
- Issue
- 2
- Pages
- 284-291
- ISSN
- 0893-228X (ISSN-L)
- 1520-5010
- OpenAlex
- W2044263529
- Cited by
- 235
- References
- 0
- FWCI
- 5.73
- Type
- journal article
- Language
- en
- Open access
- closed
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