Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines

Giovanna Zolese, Giancarlo Falcioni, Enrico Bertoli, Roberta Galeazzi, Michal Wozniak, Zbigniew Wypych, Enrico Gratton, Annarina Ambrosini

Research output: Contribution to journalArticlepeer-review

Abstract

The functions of N-acylethanolamines, minor constituents of mammalian cells, are poorly understood. It was suggested that NAEs might have some pharmacological actions and might serve as a cytoprotective response, whether mediated by physical interactions with membranes or enzymes or mediated by activation of cannabinoid receptors. Albumins are identified as the major transport proteins in blood plasma for many compounds including fatty acids, hormones, bilirubin, ions, and many drugs. Moreover, albumin has been used as a model protein in many areas, because of its multifunctional binding properties. Bovine (BSA) and human (HSA) serum albumin are similar in sequence and conformation, but differ for the number of tryptophan residues. This difference can be used to monitor unlike protein domains. Our data suggest that NOEA binds with high affinity to both albumins, modifying their conformational features. In both proteins, NOEA molecules are linked with higher affinity to hydrophobic sites near Trp-214 in HSA or Trp-212 in BSA. Moreover, fluorescence data support the hypothesis of the presence of other NOEA binding sites on BSA, likely affecting Trp-134 environment. The presence of similar binding sites is not measurable on HSA, because it lacks of the second Trp residue. (C) 2000 Wiley-Liss, Inc.

Original languageEnglish
Pages (from-to)39-48
Number of pages10
JournalProteins: Structure, Function and Genetics
Volume40
Issue number1
DOIs
Publication statusPublished - Jul 1 2000

Keywords

  • Albumin
  • Circular dichroism
  • Fluorescence
  • N-acylethanolamine

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

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