Blog
About

  • Record: found
  • Abstract: found
  • Article: not found

Observation of a new nonfluorescent malondialdehyde-acetaldehyde-protein adduct by 13C NMR spectroscopy.

Read this article at

ScienceOpenPublisherPubMed
Bookmark
      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

      Abstract

      It has been shown that malondialdehyde (MDA) and acetaldehyde react with proteins via the epsilon-amino group of a lysine residue to yield hybrid MDA-acetaldehyde (MAA)-protein adducts. The structure of one MAA adduct has been confirmed to be 4-methyl-1, 4-dihydropyridine-3,5-dicarbaldehyde (3). In this study, 13C NMR spectroscopy was used to identify the structure of a second MAA adduct as 2-formyl-3-(alkylamino)butanal (4). Isotopically labeled [1-13C]acetaldehyde was reacted with MDA and the protein, bovine serum albumin, under a variety of conditions, and the reactions were monitored at various time intervals by 13C NMR. In each experiment, new signals grew in at 50 and 22 ppm. By comparison to model compounds, the signals at 50 ppm correspond to a 2-formyl-3-(alkylamino)butanal adduct and the signals at 22 ppm correspond to the known 1,4-dihydropyridine-3,5-dicarbaldehyde adduct. Similar results were found when the BSA was replaced with polylysine. Overall, it appears that MAA-protein adducts are composed of two major products, 3 and 4.

      Related collections

      Author and article information

      Affiliations
      [1 ] Department of Chemistry, Creighton University, Omaha, Nebraska 68178, USA.
      Journal
      Chem. Res. Toxicol.
      Chemical research in toxicology
      American Chemical Society (ACS)
      0893-228X
      0893-228X
      Jan 1999
      : 12
      : 1
      9894024
      10.1021/tx980132u
      tx980132u

      Comments

      Comment on this article