Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose
Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression a...
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todo:paper_00062960_v48_n4_p786_DiLella2023-10-03T14:04:30Z Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose Di Lella, S. Ma, L. Díaz Ricci, J.C. Rabinovich, G.A. Asher, S.A. Álvarez, R.M.S. Binding proteins Carbohydrate ligands Carbohydrate-recognition domains Disaccharide lactose Galectin-1 Glycoconjugates Immune cells Inflammatory response Ligand bindings Molecular dynamic simulations Physico-chemical properties Radial distribution functions Role of waters Solvent environments Solvent reorganizations Structural changes Synthetic inhibitors Tumor progressions Uv-raman spectrum Uv-resonance raman spectroscopies Amino acids Biochemistry Ligands Molecular dynamics Organic compounds Polysaccharides Raman scattering Raman spectroscopy Sugars Distribution functions carbohydrate disaccharide galectin 1 glycan lactose solvent tryptophan LGALS1 protein, human solvent water article genetic conservation homeostasis human immunocompetent cell inflammation ligand binding molecular dynamics nonhuman physical chemistry priority journal protein carbohydrate interaction protein family Raman spectrometry tumor growth chemical model chemistry comparative study computer simulation metabolism protein binding thermodynamics X ray crystallography Computer Simulation Crystallography, X-Ray Galectin 1 Humans Lactose Models, Chemical Protein Binding Solvents Spectrum Analysis, Raman Thermodynamics Water Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1 - saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes. © 2009 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v48_n4_p786_DiLella |
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Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Binding proteins Carbohydrate ligands Carbohydrate-recognition domains Disaccharide lactose Galectin-1 Glycoconjugates Immune cells Inflammatory response Ligand bindings Molecular dynamic simulations Physico-chemical properties Radial distribution functions Role of waters Solvent environments Solvent reorganizations Structural changes Synthetic inhibitors Tumor progressions Uv-raman spectrum Uv-resonance raman spectroscopies Amino acids Biochemistry Ligands Molecular dynamics Organic compounds Polysaccharides Raman scattering Raman spectroscopy Sugars Distribution functions carbohydrate disaccharide galectin 1 glycan lactose solvent tryptophan LGALS1 protein, human solvent water article genetic conservation homeostasis human immunocompetent cell inflammation ligand binding molecular dynamics nonhuman physical chemistry priority journal protein carbohydrate interaction protein family Raman spectrometry tumor growth chemical model chemistry comparative study computer simulation metabolism protein binding thermodynamics X ray crystallography Computer Simulation Crystallography, X-Ray Galectin 1 Humans Lactose Models, Chemical Protein Binding Solvents Spectrum Analysis, Raman Thermodynamics Water |
| spellingShingle |
Binding proteins Carbohydrate ligands Carbohydrate-recognition domains Disaccharide lactose Galectin-1 Glycoconjugates Immune cells Inflammatory response Ligand bindings Molecular dynamic simulations Physico-chemical properties Radial distribution functions Role of waters Solvent environments Solvent reorganizations Structural changes Synthetic inhibitors Tumor progressions Uv-raman spectrum Uv-resonance raman spectroscopies Amino acids Biochemistry Ligands Molecular dynamics Organic compounds Polysaccharides Raman scattering Raman spectroscopy Sugars Distribution functions carbohydrate disaccharide galectin 1 glycan lactose solvent tryptophan LGALS1 protein, human solvent water article genetic conservation homeostasis human immunocompetent cell inflammation ligand binding molecular dynamics nonhuman physical chemistry priority journal protein carbohydrate interaction protein family Raman spectrometry tumor growth chemical model chemistry comparative study computer simulation metabolism protein binding thermodynamics X ray crystallography Computer Simulation Crystallography, X-Ray Galectin 1 Humans Lactose Models, Chemical Protein Binding Solvents Spectrum Analysis, Raman Thermodynamics Water Di Lella, S. Ma, L. Díaz Ricci, J.C. Rabinovich, G.A. Asher, S.A. Álvarez, R.M.S. Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| topic_facet |
Binding proteins Carbohydrate ligands Carbohydrate-recognition domains Disaccharide lactose Galectin-1 Glycoconjugates Immune cells Inflammatory response Ligand bindings Molecular dynamic simulations Physico-chemical properties Radial distribution functions Role of waters Solvent environments Solvent reorganizations Structural changes Synthetic inhibitors Tumor progressions Uv-raman spectrum Uv-resonance raman spectroscopies Amino acids Biochemistry Ligands Molecular dynamics Organic compounds Polysaccharides Raman scattering Raman spectroscopy Sugars Distribution functions carbohydrate disaccharide galectin 1 glycan lactose solvent tryptophan LGALS1 protein, human solvent water article genetic conservation homeostasis human immunocompetent cell inflammation ligand binding molecular dynamics nonhuman physical chemistry priority journal protein carbohydrate interaction protein family Raman spectrometry tumor growth chemical model chemistry comparative study computer simulation metabolism protein binding thermodynamics X ray crystallography Computer Simulation Crystallography, X-Ray Galectin 1 Humans Lactose Models, Chemical Protein Binding Solvents Spectrum Analysis, Raman Thermodynamics Water |
| description |
Galectin-1 (Gal-1), a member of a family of evolutionarily conserved glycan-binding proteins, binds specifically to poly-N-acetyllactosamine-enriched glycoconjugates. Through interactions with these glycoconjugates, this protein modulates inflammatory responses and contributes to tumor progression and immune cell homeostasis. The carbohydrate recognition domain includes the single protein tryptophan (Trp68). UV resonance Raman spectroscopy and molecular dynamic simulation were used to examine the change in the environment of the Trp on ligand binding. The UV Raman spectra and the calculated water radial distribution functions show that, while no large structural changes in the protein follow lactose binding, substantial solvent reorganization occurs. These new insights into the microscopic role of water molecules in Gal-1 binding to its specific carbohydrate ligands provides a better understanding of the physicochemical properties of Gal-1 - saccharide interactions, which will be useful for the design of synthetic inhibitors for therapeutic purposes. © 2009 American Chemical Society. |
| format |
JOUR |
| author |
Di Lella, S. Ma, L. Díaz Ricci, J.C. Rabinovich, G.A. Asher, S.A. Álvarez, R.M.S. |
| author_facet |
Di Lella, S. Ma, L. Díaz Ricci, J.C. Rabinovich, G.A. Asher, S.A. Álvarez, R.M.S. |
| author_sort |
Di Lella, S. |
| title |
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| title_short |
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| title_full |
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| title_fullStr |
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| title_full_unstemmed |
Critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| title_sort |
critical role of the solvent environment in galectin-1 binding to the disaccharide lactose |
| url |
http://hdl.handle.net/20.500.12110/paper_00062960_v48_n4_p786_DiLella |
| work_keys_str_mv |
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