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Mariella Tegoni - One of the best experts on this subject based on the ideXlab platform.
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Deswapping bovine odorant binding Protein.
Biochimica et biophysica acta, 2008Co-Authors: Roberto Ramoni, Stefano Grolli, Virna Conti, Silvia Spinelli, Christian Cambillau, E. Merli, Mariella TegoniAbstract:The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121. This mutation yielded a monomeric bOBP-121Gly+ in which domain swapping has been reverted. Here, we have subsequently introduced two mutations, Trp64Cys and His155Cys, in view to stabilize the putative monomer with a disulfide bridge. We have determined the crystal structure of this triple mutant at 1.65 A resolution. The mutant Protein is monomeric, stabilized by a disulfide bridge between Trp64Cys and His155Cys, with a backbone superimposable to that of native bOBP, with the exception of the hinge and of the 10 residues at the C-terminus. bOBP triple mutant binds 1-amino-anthracene, 1-octen-3-ol (bOBP co-purified ligand) and other ligands with microM Kd values comparable to those of the swapped dimer.
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine Odorant-Binding Protein
Journal of Biological Chemistry, 2001Co-Authors: Roberto Ramoni, Patricia Nagnan-le Meillour, Florence Vincent, Stefano Grolli, Virna Conti, Christian Malosse, Silvia Spinelli, Christian Cambillau, Francois Boyer, Mariella TegoniAbstract:Bovine Odorant-Binding Protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors likeAnopheles (Plasmodium) or Glossina(Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.
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The insect attractant 1-octen-3-ol is the natural ligand of bovine Odorant-Binding Protein.
The Journal of biological chemistry, 2000Co-Authors: Roberto Ramoni, Florence Vincent, Stefano Grolli, Virna Conti, Christian Malosse, François-didier Boyer, Patricia Nagnan-le Meillour, Silvia Spinelli, Christian Cambillau, Mariella TegoniAbstract:Bovine Odorant-Binding Protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.
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complexes of porcine odorant binding Protein with odorant molecules belonging to different chemical classes
Journal of Molecular Biology, 2000Co-Authors: Florence Vincent, Paolo Pelosi, Roberto Ramoni, Stefano Grolli, Silvia Spinelli, Christian Cambillau, Mariella TegoniAbstract:Porcine odorant binding Protein (pOBP) is a monomer of 157 amino acid residues, purified in abundance from pig nasal mucosa. In contrast to the observation on lipocalins as retinol binding Protein (RBP), major urinary Protein (MUP) or bovine odorant binding Protein (bOBP), no naturally occurring ligand was found in the β-barrel cavity of pOBP. Porcine OBP was therefore chosen as a simple model for structure/function studies with odorant molecules. In competition experiments with tritiated pyrazine, the affinity of pOBP towards several odorant molecules belonging to different chemical classes has been found to be of the micromolar order, with a 1:1 stoichiometry. The X-ray structures of pOBP complexed to these molecules were determined at resolution between 2.15 and 1.4 A. As expected, the electron density of the odorant molecules was observed into the hydrophobic β-barrel of the lipocalin. Inside this cavity, very few specific interactions were established between the odorant molecule and the amino acid side-chains, which did not undergo significant conformational change. The high B-factors observed for the odorant molecules as well as the existence of alternative conformations reveal a non-specific mode of binding of the odorant molecules in the cavity.
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molecular cloning and bacterial expression of a general odorant binding Protein from the cabbage armyworm mamestra brassicae
FEBS Journal, 1998Co-Authors: Martine Maibechecoisne, Christian Cambillau, Mariella Tegoni, Sonia Longhi, Emmanuelle Jacquinjoly, Carole Brunel, Mariepierre Egloff, Louis N Gastinel, Patricia Nagnan-le MeillourAbstract:A cDNA clone encoding a general Odorant-Binding Protein (GOBP2) was isolated from antennal RNA of Mamestra brassicae by reverse transcription-PCR (RT-PCR) and RACE-PCR. The cDNA encoding the GOBP2 was further used for bacterial expression. Most of the recombinant GOBP2 (.90 %) was found to be insoluble. Purification under denaturing conditions consisted of solubilisation of inclusion bodies, affinity chromatography, refolding and gel filtration. The refolded rGOBP2 was cross-reactive with a serum raised against the GOBP2 of the Lepidoptera Antheraea polyphemus. The purified refolded rGOBP2 was further characterised by native PAGE, IEF, N-terminal sequencing, and two-dimensional NMR. A functional characterisation of the rGOBP2 was carried out by testing its ability to bind phero- mone compounds. The yields of production and purification fulfil the requirements of structural studies.
Loïc Briand - One of the best experts on this subject based on the ideXlab platform.
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A conserved odorant binding Protein is required for essential amino acid detection in Drosophila
Communications Biology, 2019Co-Authors: Karen Rihani, Stéphane Fraichard, Isabelle Chauvel, Nicolas Poirier, Thomas Delompré, Fabrice Neiers, Teiichi Tanimura, Jean-françois Ferveur, Loïc BriandAbstract:Animals need to detect in the food essential amino acids that they cannot synthesize. We found that the odorant binding Protein OBP19b, which is highly expressed in Drosophila melanogaster taste sensilla, is necessary for the detection of several amino acids including the essential l-phenylalanine. The recombinant OBP19b Protein was produced and characterized for its binding properties: it stereoselectively binds to several amino acids. Using a feeding-choice assay, we found that OBP19b is necessary for detecting l-phenylalanine and l-glutamine, but not l-alanine or D-phenylalanine. We mapped the cells expressing OBP19b and compared the electrophysiological responses of a single taste sensillum to several amino acids: OBP19b mutant flies showed a reduced response compared to control flies when tested to preferred amino acids, but not to the other ones. OBP19b is well conserved in phylogenetically distant species suggesting that this Protein is necessary for detection of specific amino acids in insects.
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A conserved odorant binding Protein is required for essential amino acid detection in Drosophila
Communications Biology, 2019Co-Authors: Karen Rihani, Stéphane Fraichard, Isabelle Chauvel, Nicolas Poirier, Thomas Delompré, Fabrice Neiers, Teiichi Tanimura, Jean-françois Ferveur, Loïc BriandAbstract:Animals need to detect in the food essential amino acids that they cannot synthesize. We found that the odorant binding Protein OBP19b, which is highly expressed in Drosophila melanogaster taste sensilla, is necessary for the detection of several amino acids including the essential l -phenylalanine. The recombinant OBP19b Protein was produced and characterized for its binding properties: it stereoselectively binds to several amino acids. Using a feeding-choice assay, we found that OBP19b is necessary for detecting l -phenylalanine and l -glutamine, but not l -alanine or D -phenylalanine. We mapped the cells expressing OBP19b and compared the electrophysiological responses of a single taste sensillum to several amino acids: OBP19b mutant flies showed a reduced response compared to control flies when tested to preferred amino acids, but not to the other ones. OBP19b is well conserved in phylogenetically distant species suggesting that this Protein is necessary for detection of specific amino acids in insects. Karen Rihani et al. demonstrate that fruit flies need an Odorant-Binding Protein OBP19b, which is highly expressed in taste sensilla, to prefer select amino acids such as essential l -phenylalanine. This study provides insights into the mechanisms by which insects ensure their dietary intake of essential amino acids.
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Interaction between odorants and Proteins involved in the perception of smell: the case of odorant‐binding Proteins probed by molecular modelling and biophysical data
Flavour and Fragrance Journal, 2012Co-Authors: Jérôme Golebiowski, Landry Charlier, Jérémie Topin, Loïc BriandAbstract:A joint approach that combines molecular modelling and fluorescence spectroscopy is used to study the affinity of an odorant binding Protein towards various odorant molecules. We focus on the capability of molecular modelling to rank odorants according to their affinity with this Protein, which is involved in the sense of smell. Although ligand-based approaches are unable to propose an accurate model attending to the strength of the bond with the Odorant-Binding Protein, receptor-based structures considering either static or dynamic structure of the Protein perform equally to discriminate between good, medium and low affinity odorants. Such approaches will be useful for further rational design of either odorants or bio-inspired sensors. Copyright © 2012 John Wiley & Sons, Ltd.
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Interaction between odorants and Proteins involved in the perception of smell: the case of Odorant-Binding Proteins probed by molecular modelling and biophysical data
Flavour and Fragrance Journal, 2012Co-Authors: Jérôme Golebiowski, Landry Charlier, Jérémie Topin, Loïc BriandAbstract:A joint approach that combines molecular modelling and fluorescence spectroscopy is used to study the affinity of an odorant binding Protein towards various odorant molecules. We focus on the capability of molecular modelling to rank odorants according to their affinity with this Protein, which is involved in the sense of smell. Although ligand-based approaches are unable to propose an accurate model attending to the strength of the bond with the Odorant-Binding Protein, receptor-based structures considering either static or dynamic structure of the Protein perform equally to discriminate between good, medium and low affinity odorants. Such approaches will be useful for further rational design of either odorants or bio-inspired sensors.
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Rapid odorant release in mammalian odour binding Proteins facilitates their temporal coupling to odorant signals
Journal of Molecular Biology, 2010Co-Authors: Antoni Borysik, Loïc Briand, Andrew Taylor, David ScottAbstract:We have measured the effect of rat Odorant-Binding Protein 1 on the rates of ligand uptake and liquid-to-air transfer rates with a set of defined odorous compounds. Comparison of observed rate constants (k(obs)) with data simulated over a wide range of different kinetic and thermodynamic regimes shows that the data do not agree with the previously held view of a slow off-rate regime (k(off)
Jihad René Albani - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp residues of three lipocalin Proteins family α1 acid glycoProtein orosomucoid β lactoglobulin and porcine odorant binding Protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp residues of α(1)-acid glycoProtein, β-lactoglobulin and porcine odorant binding Protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three Proteins inducing a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic tryptophan residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp residues are far from the pocket and to α(1)-acid glycoProtein where three Trp residues are present at different areas of the Protein.
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energy transfer studies between trp residues of three lipocalin Proteins family α1 acid glycoProtein orosomucoid β lactoglobulin and porcine odorant binding Protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp residues of α1-acid glycoProtein, β-lactoglobulin and porcine odorant binding Protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three Proteins inducing a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic tryptophan residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp residues are far from the pocket and to α1-acid glycoProtein where three Trp residues are present at different areas of the Protein.
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effect of 1 aminoanthracene 1 ama binding on the structure of three lipocalin Proteins the dimeric β lactoglobulin the dimeric odorant binding Protein and the monomeric α1 acid glycoProtein fluorescence spectra and lifetimes studies
Journal of Fluorescence, 2010Co-Authors: Daniel Kmiecik, Jihad René AlbaniAbstract:We studied effect of 1-aminoanthracene (1-AMA) binding on the structures of dimeric β lactoglobulin, dimeric odorant binding Protein (OBP) and monomeric α(1)-acid glycoProtein (lipocalin family Proteins) by monitoring fluorescence excitation spectra and measuring fluorescence lifetimes of the tryptophan residues of the Proteins. Results show that binding of 1-AMA to β lactoglobulin and OBP modifies their conformation even at low probe concentration compared to that of the Proteins. Structural modification induces a red shift of the fluorescence excitation spectra maximum of tryptophan residues accompanied with an increase of the third fluorescence lifetime and a decrease of its pre-exponential factor. These effects were not observed for α(1)-acid glycoProtein, probably as the result of carbohydrate presence. These data raise doubts concerning use of 1-AMA as a probe to study biological properties of β lactoglobulin and OBP.
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Fluorescence properties of porcine odorant binding Protein Trp 16 residue
Journal of Luminescence, 2010Co-Authors: Jihad René AlbaniAbstract:Summary The present work deals with fluorescence studies of adult porcine odorant binding Protein at pH=7.5. At this pH, the Protein is a dimer, each monomer contains one tryptophan residue. Our results show that tryptophan residue displays significant motions and emits with three fluorescence lifetimes. Decay associated spectra showed that the three lifetime’s components emanate from sub-structures surrounded by the same microenvironment.
Roberto Ramoni - One of the best experts on this subject based on the ideXlab platform.
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Characterization of a deswapped triple mutant bovine odorant binding Protein.
International journal of molecular sciences, 2011Co-Authors: Eugenia Polverini, R. T. Sorbi, Roberto Ramoni, Paolo Lardi, Alberto Mazzini, Conti Virna, Roberto FavillaAbstract:The stability and functionality of GCC-bOBP, a monomeric triple mutant of bovine odorant binding Protein, was investigated, in the presence of denaturant and in acidic pH conditions, by both Protein and 1-aminoanthracene ligand fluorescence measurements, and compared to that of both bovine and porcine wild type homologues. Complete reversibility of unfolding was observed, though refolding was characterized by hysteresis. Molecular dynamics simulations, performed to detect possible structural changes of the monomeric scaffold related to the presence of the ligand, pointed out the stability of the β-barrel lipocalin scaffold.
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Deswapping bovine odorant binding Protein.
Biochimica et biophysica acta, 2008Co-Authors: Roberto Ramoni, Stefano Grolli, Virna Conti, Silvia Spinelli, Christian Cambillau, E. Merli, Mariella TegoniAbstract:The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121. This mutation yielded a monomeric bOBP-121Gly+ in which domain swapping has been reverted. Here, we have subsequently introduced two mutations, Trp64Cys and His155Cys, in view to stabilize the putative monomer with a disulfide bridge. We have determined the crystal structure of this triple mutant at 1.65 A resolution. The mutant Protein is monomeric, stabilized by a disulfide bridge between Trp64Cys and His155Cys, with a backbone superimposable to that of native bOBP, with the exception of the hinge and of the 10 residues at the C-terminus. bOBP triple mutant binds 1-amino-anthracene, 1-octen-3-ol (bOBP co-purified ligand) and other ligands with microM Kd values comparable to those of the swapped dimer.
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine Odorant-Binding Protein
Journal of Biological Chemistry, 2001Co-Authors: Roberto Ramoni, Patricia Nagnan-le Meillour, Florence Vincent, Stefano Grolli, Virna Conti, Christian Malosse, Silvia Spinelli, Christian Cambillau, Francois Boyer, Mariella TegoniAbstract:Bovine Odorant-Binding Protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors likeAnopheles (Plasmodium) or Glossina(Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.
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The insect attractant 1-octen-3-ol is the natural ligand of bovine Odorant-Binding Protein.
The Journal of biological chemistry, 2000Co-Authors: Roberto Ramoni, Florence Vincent, Stefano Grolli, Virna Conti, Christian Malosse, François-didier Boyer, Patricia Nagnan-le Meillour, Silvia Spinelli, Christian Cambillau, Mariella TegoniAbstract:Bovine Odorant-Binding Protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-A resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996) Nat. Struct. Biol. 3, 863-867; Bianchet et al. (1996) Nat. Struct. Biol. 3, 934-939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-A resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body emanations of humans and animals. The compound 1-octen-3-ol is also an extremely potent olfactory attractant for many insect species, including some parasite vectors like Anopheles (Plasmodium) or Glossina (Trypanosoma). For the first time, a function can be assigned to an OBP, with a possible role of bOBP in the ecological relationships between bovine and insect species.
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complexes of porcine odorant binding Protein with odorant molecules belonging to different chemical classes
Journal of Molecular Biology, 2000Co-Authors: Florence Vincent, Paolo Pelosi, Roberto Ramoni, Stefano Grolli, Silvia Spinelli, Christian Cambillau, Mariella TegoniAbstract:Porcine odorant binding Protein (pOBP) is a monomer of 157 amino acid residues, purified in abundance from pig nasal mucosa. In contrast to the observation on lipocalins as retinol binding Protein (RBP), major urinary Protein (MUP) or bovine odorant binding Protein (bOBP), no naturally occurring ligand was found in the β-barrel cavity of pOBP. Porcine OBP was therefore chosen as a simple model for structure/function studies with odorant molecules. In competition experiments with tritiated pyrazine, the affinity of pOBP towards several odorant molecules belonging to different chemical classes has been found to be of the micromolar order, with a 1:1 stoichiometry. The X-ray structures of pOBP complexed to these molecules were determined at resolution between 2.15 and 1.4 A. As expected, the electron density of the odorant molecules was observed into the hydrophobic β-barrel of the lipocalin. Inside this cavity, very few specific interactions were established between the odorant molecule and the amino acid side-chains, which did not undergo significant conformational change. The high B-factors observed for the odorant molecules as well as the existence of alternative conformations reveal a non-specific mode of binding of the odorant molecules in the cavity.
Daniel Kmiecik - One of the best experts on this subject based on the ideXlab platform.
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energy transfer studies between trp residues of three lipocalin Proteins family α1 acid glycoProtein orosomucoid β lactoglobulin and porcine odorant binding Protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp residues of α1-acid glycoProtein, β-lactoglobulin and porcine odorant binding Protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three Proteins inducing a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic tryptophan residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp residues are far from the pocket and to α1-acid glycoProtein where three Trp residues are present at different areas of the Protein.
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energy transfer studies between trp residues of three lipocalin Proteins family α1 acid glycoProtein orosomucoid β lactoglobulin and porcine odorant binding Protein and the fluorescent probe 1 aminoanthracene 1 ama
Journal of Fluorescence, 2015Co-Authors: Jihad René Albani, Loic Bretesche, Julie Vogelaer, Daniel KmiecikAbstract:Energy transfer studies between Trp residues of α(1)-acid glycoProtein, β-lactoglobulin and porcine odorant binding Protein (OBP) and the fluorescent probe 1-aminoanthracene (1-AMA) were performed. 1-AMA binds to the hydrophobic binding sites of the three Proteins inducing a decrease in the fluorescence intensity of the Trp residues accompanied by an increase of that of 1-AMA. Our results indicate that 1-AMA is in close contact with hydrophobic tryptophan residue of β-lactoglobulin (Trp 19) to the difference of its binding to OBP, where Trp residues are far from the pocket and to α(1)-acid glycoProtein where three Trp residues are present at different areas of the Protein.
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effect of 1 aminoanthracene 1 ama binding on the structure of three lipocalin Proteins the dimeric β lactoglobulin the dimeric odorant binding Protein and the monomeric α1 acid glycoProtein fluorescence spectra and lifetimes studies
Journal of Fluorescence, 2010Co-Authors: Daniel Kmiecik, Jihad René AlbaniAbstract:We studied effect of 1-aminoanthracene (1-AMA) binding on the structures of dimeric β lactoglobulin, dimeric odorant binding Protein (OBP) and monomeric α(1)-acid glycoProtein (lipocalin family Proteins) by monitoring fluorescence excitation spectra and measuring fluorescence lifetimes of the tryptophan residues of the Proteins. Results show that binding of 1-AMA to β lactoglobulin and OBP modifies their conformation even at low probe concentration compared to that of the Proteins. Structural modification induces a red shift of the fluorescence excitation spectra maximum of tryptophan residues accompanied with an increase of the third fluorescence lifetime and a decrease of its pre-exponential factor. These effects were not observed for α(1)-acid glycoProtein, probably as the result of carbohydrate presence. These data raise doubts concerning use of 1-AMA as a probe to study biological properties of β lactoglobulin and OBP.
