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 journalArticle

90 Citations (Scopus)

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

Fingerprint

Albumins
Fluorescence
Binding Sites
Cannabinoid Receptors
Proteins
Bilirubin
Serum Albumin
Tryptophan
Conformations
Carrier Proteins
Blood
Fatty Acids
Chemical activation
Cells
Hormones
Pharmacology
Ions
Membranes
Plasmas
Molecules

Keywords

  • Albumin
  • Circular dichroism
  • Fluorescence
  • N-acylethanolamine

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

Cite this

Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines. / Zolese, Giovanna; Falcioni, Giancarlo; Bertoli, Enrico; Galeazzi, Roberta; Wozniak, Michal; Wypych, Zbigniew; Gratton, Enrico; Ambrosini, Annarina.

In: Proteins: Structure, Function and Genetics, Vol. 40, No. 1, 01.07.2000, p. 39-48.

Research output: Contribution to journalArticle

Zolese, Giovanna ; Falcioni, Giancarlo ; Bertoli, Enrico ; Galeazzi, Roberta ; Wozniak, Michal ; Wypych, Zbigniew ; Gratton, Enrico ; Ambrosini, Annarina. / Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines. In: Proteins: Structure, Function and Genetics. 2000 ; Vol. 40, No. 1. pp. 39-48.
@article{6a82b1fa05a84a92bd1b1d58450fb391,
title = "Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines",
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.",
keywords = "Albumin, Circular dichroism, Fluorescence, N-acylethanolamine",
author = "Giovanna Zolese and Giancarlo Falcioni and Enrico Bertoli and Roberta Galeazzi and Michal Wozniak and Zbigniew Wypych and Enrico Gratton and Annarina Ambrosini",
year = "2000",
month = "7",
day = "1",
doi = "10.1002/(SICI)1097-0134(20000701)40:1<39::AID-PROT60>3.0.CO;2-N",
language = "English",
volume = "40",
pages = "39--48",
journal = "Proteins: Structure, Function and Genetics",
issn = "0887-3585",
publisher = "Wiley-Liss Inc.",
number = "1",

}

TY - JOUR

T1 - Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines

AU - Zolese, Giovanna

AU - Falcioni, Giancarlo

AU - Bertoli, Enrico

AU - Galeazzi, Roberta

AU - Wozniak, Michal

AU - Wypych, Zbigniew

AU - Gratton, Enrico

AU - Ambrosini, Annarina

PY - 2000/7/1

Y1 - 2000/7/1

N2 - 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.

AB - 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.

KW - Albumin

KW - Circular dichroism

KW - Fluorescence

KW - N-acylethanolamine

UR - http://www.scopus.com/inward/record.url?scp=0034237803&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034237803&partnerID=8YFLogxK

U2 - 10.1002/(SICI)1097-0134(20000701)40:1<39::AID-PROT60>3.0.CO;2-N

DO - 10.1002/(SICI)1097-0134(20000701)40:1<39::AID-PROT60>3.0.CO;2-N

M3 - Article

C2 - 10813829

AN - SCOPUS:0034237803

VL - 40

SP - 39

EP - 48

JO - Proteins: Structure, Function and Genetics

JF - Proteins: Structure, Function and Genetics

SN - 0887-3585

IS - 1

ER -