Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria

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The stability of proteins involves a critical balance of interactions of different orders of magnitude. In this work, we present experimental evidence of an increased thermal stability of galectin-1, a multifunctional β-galactoside-binding protein, upon binding to the disaccharide lactose. Analysis...

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Autores principales:	Di Lella, S., Martí, M.A., Croci, D.O., Guardia, C.M.A., Díaz-Ricci, J.C., Rabinovich, G.A., Caramelo, J.J., Estrin, D.A.
Formato:	JOUR
Materias:	Biological systems Dichroism Dimerization Ligands Molecular dynamics Proteins Sugars Thermodynamic stability Binding proteins Biological functions Circular dichroism Conformational entropy Different order Disaccharide lactose Experimental evidence Galectin-1 Glycans Internal energies Ligand binding Molecular dynamics simulations Physicochemical property Solvation free energies Structural change Therapeutic Application Thermal denaturations Thermal stability Binding energy beta galactoside carbohydrate binding protein disaccharide galectin 1 glycan lactose lectin recombinant protein beta-galactoside galactoside ligand article bacterial cell circular dichroism dimerization energy entropy Escherichia coli human ligand binding molecular dynamics nonhuman priority journal protein denaturation protein structure spectroscopy structure analysis thermodynamics thermostability binding site chemical structure chemistry metabolism protein folding Binding Sites Galactosides Galectin 1 Humans Models, Molecular Protein Folding Thermodynamics
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00062960_v49_n35_p7652_DiLella
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00062960_v49_n35_p7652_DiLella
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spelling	todo:paper_00062960_v49_n35_p7652_DiLella2023-10-03T14:04:31Z Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria Di Lella, S. Martí, M.A. Croci, D.O. Guardia, C.M.A. Díaz-Ricci, J.C. Rabinovich, G.A. Caramelo, J.J. Estrin, D.A. Biological systems Dichroism Dimerization Ligands Molecular dynamics Proteins Sugars Thermodynamic stability Binding proteins Biological functions Circular dichroism Conformational entropy Different order Disaccharide lactose Experimental evidence Galectin-1 Glycans Internal energies Ligand binding Molecular dynamics simulations Physicochemical property Solvation free energies Structural change Therapeutic Application Thermal denaturations Thermal stability Binding energy beta galactoside carbohydrate binding protein disaccharide galectin 1 glycan lactose lectin recombinant protein beta-galactoside galactoside galectin 1 ligand article bacterial cell circular dichroism dimerization energy entropy Escherichia coli human ligand binding molecular dynamics nonhuman priority journal protein denaturation protein structure spectroscopy structure analysis thermodynamics thermostability binding site chemical structure chemistry metabolism protein folding Binding Sites Dimerization Galactosides Galectin 1 Humans Ligands Models, Molecular Protein Folding Thermodynamics The stability of proteins involves a critical balance of interactions of different orders of magnitude. In this work, we present experimental evidence of an increased thermal stability of galectin-1, a multifunctional β-galactoside-binding protein, upon binding to the disaccharide lactose. Analysis of structural changes occurring upon binding of lectin to its specific glycans and thermal denaturation of the protein and the complex were analyzed by circular dichroism. On the other hand, we studied dimerization as another factor that may induce structural and thermal stability changes. The results were then complemented with molecular dynamics simulations followed by a detailed computation of thermodynamic properties, including the internal energy, solvation free energy, and conformational entropy. In addition, an energetic profile of the binding and dimerization processes is also presented. Whereas binding and cross-linking of lactose do not alter galectin-1 structure, this interaction leads to substantial changes in the flexibility and internal energy of the protein which confers increased thermal stability to this endogenous lectin. Given that an improved understanding of the physicochemical properties of galectin-glycan lattices may contribute to the dissection of their biological functions and prediction of their therapeutic applications, our study suggests that galectin binding to specific disaccharide ligands may increase the thermal stability of this glycan-binding protein, an effect that could influence its critical biological functions. © 2010 American Chemical Society. Fil:Martí, M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Croci, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Guardia, C.M.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v49_n35_p7652_DiLella
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Biological systems Dichroism Dimerization Ligands Molecular dynamics Proteins Sugars Thermodynamic stability Binding proteins Biological functions Circular dichroism Conformational entropy Different order Disaccharide lactose Experimental evidence Galectin-1 Glycans Internal energies Ligand binding Molecular dynamics simulations Physicochemical property Solvation free energies Structural change Therapeutic Application Thermal denaturations Thermal stability Binding energy beta galactoside carbohydrate binding protein disaccharide galectin 1 glycan lactose lectin recombinant protein beta-galactoside galactoside galectin 1 ligand article bacterial cell circular dichroism dimerization energy entropy Escherichia coli human ligand binding molecular dynamics nonhuman priority journal protein denaturation protein structure spectroscopy structure analysis thermodynamics thermostability binding site chemical structure chemistry metabolism protein folding Binding Sites Dimerization Galactosides Galectin 1 Humans Ligands Models, Molecular Protein Folding Thermodynamics
spellingShingle	Biological systems Dichroism Dimerization Ligands Molecular dynamics Proteins Sugars Thermodynamic stability Binding proteins Biological functions Circular dichroism Conformational entropy Different order Disaccharide lactose Experimental evidence Galectin-1 Glycans Internal energies Ligand binding Molecular dynamics simulations Physicochemical property Solvation free energies Structural change Therapeutic Application Thermal denaturations Thermal stability Binding energy beta galactoside carbohydrate binding protein disaccharide galectin 1 glycan lactose lectin recombinant protein beta-galactoside galactoside galectin 1 ligand article bacterial cell circular dichroism dimerization energy entropy Escherichia coli human ligand binding molecular dynamics nonhuman priority journal protein denaturation protein structure spectroscopy structure analysis thermodynamics thermostability binding site chemical structure chemistry metabolism protein folding Binding Sites Dimerization Galactosides Galectin 1 Humans Ligands Models, Molecular Protein Folding Thermodynamics Di Lella, S. Martí, M.A. Croci, D.O. Guardia, C.M.A. Díaz-Ricci, J.C. Rabinovich, G.A. Caramelo, J.J. Estrin, D.A. Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
topic_facet	Biological systems Dichroism Dimerization Ligands Molecular dynamics Proteins Sugars Thermodynamic stability Binding proteins Biological functions Circular dichroism Conformational entropy Different order Disaccharide lactose Experimental evidence Galectin-1 Glycans Internal energies Ligand binding Molecular dynamics simulations Physicochemical property Solvation free energies Structural change Therapeutic Application Thermal denaturations Thermal stability Binding energy beta galactoside carbohydrate binding protein disaccharide galectin 1 glycan lactose lectin recombinant protein beta-galactoside galactoside galectin 1 ligand article bacterial cell circular dichroism dimerization energy entropy Escherichia coli human ligand binding molecular dynamics nonhuman priority journal protein denaturation protein structure spectroscopy structure analysis thermodynamics thermostability binding site chemical structure chemistry metabolism protein folding Binding Sites Dimerization Galactosides Galectin 1 Humans Ligands Models, Molecular Protein Folding Thermodynamics
description	The stability of proteins involves a critical balance of interactions of different orders of magnitude. In this work, we present experimental evidence of an increased thermal stability of galectin-1, a multifunctional β-galactoside-binding protein, upon binding to the disaccharide lactose. Analysis of structural changes occurring upon binding of lectin to its specific glycans and thermal denaturation of the protein and the complex were analyzed by circular dichroism. On the other hand, we studied dimerization as another factor that may induce structural and thermal stability changes. The results were then complemented with molecular dynamics simulations followed by a detailed computation of thermodynamic properties, including the internal energy, solvation free energy, and conformational entropy. In addition, an energetic profile of the binding and dimerization processes is also presented. Whereas binding and cross-linking of lactose do not alter galectin-1 structure, this interaction leads to substantial changes in the flexibility and internal energy of the protein which confers increased thermal stability to this endogenous lectin. Given that an improved understanding of the physicochemical properties of galectin-glycan lattices may contribute to the dissection of their biological functions and prediction of their therapeutic applications, our study suggests that galectin binding to specific disaccharide ligands may increase the thermal stability of this glycan-binding protein, an effect that could influence its critical biological functions. © 2010 American Chemical Society.
format	JOUR
author	Di Lella, S. Martí, M.A. Croci, D.O. Guardia, C.M.A. Díaz-Ricci, J.C. Rabinovich, G.A. Caramelo, J.J. Estrin, D.A.
author_facet	Di Lella, S. Martí, M.A. Croci, D.O. Guardia, C.M.A. Díaz-Ricci, J.C. Rabinovich, G.A. Caramelo, J.J. Estrin, D.A.
author_sort	Di Lella, S.
title	Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
title_short	Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
title_full	Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
title_fullStr	Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
title_full_unstemmed	Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
title_sort	linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria
url	http://hdl.handle.net/20.500.12110/paper_00062960_v49_n35_p7652_DiLella
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_version_	1807316325951864832

Linking the structure and thermal stability of β-galactoside-binding protein galectin-1 to ligand binding and dimerization equilibria

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