Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction
A comparative thermodynamic study of the interaction of anilinonaphthalene sulfonate (ANS) derivatives with bovine serum albumin (BSA) was performed by using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The chemically related ligands, 1,8-ANS and 2,6-ANS, prese...
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todo:paper_15709639_v1750_n2_p122_Celej2023-10-03T16:26:53Z Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction Celej, M.S. Dassie, S.A. Freire, E. Bianconi, M.L. Fidelio, G.D. ANS derivative Linked equilibria Protein stability Protein unfolding thermodynamics Protein-ligand interaction 8 anilino 1 naphthalenesulfonic acid albumin article binding affinity differential scanning calorimetry electricity energy transfer entropy force hydrophobicity isothermal titration calorimetry mathematical computing priority journal protein conformation protein domain protein interaction simulation thermodynamics thermography thermostability validation process Anilino Naphthalenesulfonates Animals Calorimetry, Differential Scanning Cattle Heat Kinetics Ligands Models, Molecular Protein Binding Protein Denaturation Protein Folding Serum Albumin, Bovine Thermodynamics Bovinae A comparative thermodynamic study of the interaction of anilinonaphthalene sulfonate (ANS) derivatives with bovine serum albumin (BSA) was performed by using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The chemically related ligands, 1,8-ANS and 2,6-ANS, present a similar affinity for BSA with different binding energetics. The analysis of the binding driving forces suggests that not only hydrophobic effect but also electrostatic interactions are relevant, even though they have been extensively used as probes for non-polar domains in proteins. Ligand association leads to an increase in protein thermostability, indicating that both dyes interact mainly with native BSA. ITC data show that 1,8-ANS and 2,6-ANS have a moderate affinity for BSA, with an association constant of around 1-9 × 105 M-1 for the high-affinity site. Ligand binding is disfavoured by conformational entropy. The theoretical model used to simulate DSC data satisfactorily reproduces experimental thermograms, validating this approach as one which provides new insights into the interaction between one or more ligands with a protein. By comparison with 1,8-ANS, 2,6-ANS appears as a more "inert" probe to assess processes which involve conformational changes in proteins. © 2005 Elsevier B.V. All rights reserved. Fil:Freire, E. 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_15709639_v1750_n2_p122_Celej |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
ANS derivative Linked equilibria Protein stability Protein unfolding thermodynamics Protein-ligand interaction 8 anilino 1 naphthalenesulfonic acid albumin article binding affinity differential scanning calorimetry electricity energy transfer entropy force hydrophobicity isothermal titration calorimetry mathematical computing priority journal protein conformation protein domain protein interaction simulation thermodynamics thermography thermostability validation process Anilino Naphthalenesulfonates Animals Calorimetry, Differential Scanning Cattle Heat Kinetics Ligands Models, Molecular Protein Binding Protein Denaturation Protein Folding Serum Albumin, Bovine Thermodynamics Bovinae |
| spellingShingle |
ANS derivative Linked equilibria Protein stability Protein unfolding thermodynamics Protein-ligand interaction 8 anilino 1 naphthalenesulfonic acid albumin article binding affinity differential scanning calorimetry electricity energy transfer entropy force hydrophobicity isothermal titration calorimetry mathematical computing priority journal protein conformation protein domain protein interaction simulation thermodynamics thermography thermostability validation process Anilino Naphthalenesulfonates Animals Calorimetry, Differential Scanning Cattle Heat Kinetics Ligands Models, Molecular Protein Binding Protein Denaturation Protein Folding Serum Albumin, Bovine Thermodynamics Bovinae Celej, M.S. Dassie, S.A. Freire, E. Bianconi, M.L. Fidelio, G.D. Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| topic_facet |
ANS derivative Linked equilibria Protein stability Protein unfolding thermodynamics Protein-ligand interaction 8 anilino 1 naphthalenesulfonic acid albumin article binding affinity differential scanning calorimetry electricity energy transfer entropy force hydrophobicity isothermal titration calorimetry mathematical computing priority journal protein conformation protein domain protein interaction simulation thermodynamics thermography thermostability validation process Anilino Naphthalenesulfonates Animals Calorimetry, Differential Scanning Cattle Heat Kinetics Ligands Models, Molecular Protein Binding Protein Denaturation Protein Folding Serum Albumin, Bovine Thermodynamics Bovinae |
| description |
A comparative thermodynamic study of the interaction of anilinonaphthalene sulfonate (ANS) derivatives with bovine serum albumin (BSA) was performed by using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The chemically related ligands, 1,8-ANS and 2,6-ANS, present a similar affinity for BSA with different binding energetics. The analysis of the binding driving forces suggests that not only hydrophobic effect but also electrostatic interactions are relevant, even though they have been extensively used as probes for non-polar domains in proteins. Ligand association leads to an increase in protein thermostability, indicating that both dyes interact mainly with native BSA. ITC data show that 1,8-ANS and 2,6-ANS have a moderate affinity for BSA, with an association constant of around 1-9 × 105 M-1 for the high-affinity site. Ligand binding is disfavoured by conformational entropy. The theoretical model used to simulate DSC data satisfactorily reproduces experimental thermograms, validating this approach as one which provides new insights into the interaction between one or more ligands with a protein. By comparison with 1,8-ANS, 2,6-ANS appears as a more "inert" probe to assess processes which involve conformational changes in proteins. © 2005 Elsevier B.V. All rights reserved. |
| format |
JOUR |
| author |
Celej, M.S. Dassie, S.A. Freire, E. Bianconi, M.L. Fidelio, G.D. |
| author_facet |
Celej, M.S. Dassie, S.A. Freire, E. Bianconi, M.L. Fidelio, G.D. |
| author_sort |
Celej, M.S. |
| title |
Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| title_short |
Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| title_full |
Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| title_fullStr |
Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| title_full_unstemmed |
Ligand-induced thermostability in proteins: Thermodynamic analysis of ANS-albumin interaction |
| title_sort |
ligand-induced thermostability in proteins: thermodynamic analysis of ans-albumin interaction |
| url |
http://hdl.handle.net/20.500.12110/paper_15709639_v1750_n2_p122_Celej |
| work_keys_str_mv |
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1807323312450174976 |