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Steady‐state and time resolved fluorescence of albumins interacting with N‐oleylethanolamine, a component of the endogenous N‐acylethanolamines
Author(s) -
Zolese Giovanna,
Falcioni Giancarlo,
Bertoli Enrico,
Galeazzi Roberta,
Wozniak Michal,
Wypych Zbigniew,
Gratton Enrico,
Ambrosini Annarina
Publication year - 2000
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(20000701)40:1<39::aid-prot60>3.0.co;2-n
Subject(s) - tryptophan , chemistry , bovine serum albumin , biochemistry , albumin , binding site , endogeny , serum albumin , receptor , human serum albumin , residue (chemistry) , fluorescence , amino acid , physics , quantum mechanics
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. Proteins 2000;40:39–48. © 2000 Wiley‐Liss, Inc.