Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate
The action of three types of co-solutes: (i) salts (NaCl, NaBr, NaI), (ii) polymer (polyethylene glycol; PEG-400, PEG-3000, PEG-20000), and (iii) sugars (sucrose, sucralose) on the complexation between bovine serum albumin (BSA) and sodium polystyrene sulfonate (NaPSS) was studied. Three critical &l...
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MDPI AG
2022-03-01
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| Series: | Polymers |
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| Online Access: | https://www.mdpi.com/2073-4360/14/6/1245 |
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| author | Matjaž Simončič Miha Lukšič |
| author_facet | Matjaž Simončič Miha Lukšič |
| author_sort | Matjaž Simončič |
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| description | The action of three types of co-solutes: (i) salts (NaCl, NaBr, NaI), (ii) polymer (polyethylene glycol; PEG-400, PEG-3000, PEG-20000), and (iii) sugars (sucrose, sucralose) on the complexation between bovine serum albumin (BSA) and sodium polystyrene sulfonate (NaPSS) was studied. Three critical <i>p</i>H parameters were extracted from the <i>p</i>H dependence of the solution’s turbidity: <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi mathvariant="normal">c</mi></msub></mrow></semantics></math></inline-formula> corresponding to the formation of the soluble complexes, <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi mathvariant="sans-serif">Φ</mi></msub></mrow></semantics></math></inline-formula> corresponding to the formation of the insoluble complexes, and <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi>opt</mi></msub></mrow></semantics></math></inline-formula> corresponding to the charge neutralization of the complexes. In the presence of salts, the formation of soluble and insoluble complexes as well as the charge neutralization of complexes was hindered, which is a consequence of the electrostatic screening of attractive interactions between BSA and NaPSS. Distinct anion-specific trends were observed in which the stabilizing effect of the salt increased in the order: NaCl < NaBr < NaI. The presence of PEG, regardless of its molecular weight, showed no measurable effect on the formation of soluble complexes. PEG-400 and PEG-3000 showed no effect on the formation of insoluble complexes, but PEG-20000 in high concentrations promoted their formation due to the molecular crowding effect. The presence of sugar molecules had little effect on BSA-NaPSS complexation. Sucralose showed a minor stabilizing effect with respect to the onset of complex formation, which was due to its propensity to the protein surface. This was confirmed by the fluorescence quenching assay (Stern-Volmer relationship) and all-atom MD simulations. This study highlights that when evaluating the modulatory effect of co-solutes on protein-polyelectrolyte interactions, (co-solute)-protein interactions and their subsequent impact on protein aggregation must also be considered. |
| first_indexed | 2024-03-09T12:52:16Z |
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| spelling | doaj.art-bdead2e8e7544af5ba27859a53b2d81e2023-11-30T22:04:38ZengMDPI AGPolymers2073-43602022-03-01146124510.3390/polym14061245Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene SulfonateMatjaž Simončič0Miha Lukšič1Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, SloveniaFaculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, SloveniaThe action of three types of co-solutes: (i) salts (NaCl, NaBr, NaI), (ii) polymer (polyethylene glycol; PEG-400, PEG-3000, PEG-20000), and (iii) sugars (sucrose, sucralose) on the complexation between bovine serum albumin (BSA) and sodium polystyrene sulfonate (NaPSS) was studied. Three critical <i>p</i>H parameters were extracted from the <i>p</i>H dependence of the solution’s turbidity: <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi mathvariant="normal">c</mi></msub></mrow></semantics></math></inline-formula> corresponding to the formation of the soluble complexes, <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi mathvariant="sans-serif">Φ</mi></msub></mrow></semantics></math></inline-formula> corresponding to the formation of the insoluble complexes, and <inline-formula><math xmlns="http://www.w3.org/1998/Math/MathML" display="inline"><semantics><mrow><mi>p</mi><msub><mi mathvariant="normal">H</mi><mi>opt</mi></msub></mrow></semantics></math></inline-formula> corresponding to the charge neutralization of the complexes. In the presence of salts, the formation of soluble and insoluble complexes as well as the charge neutralization of complexes was hindered, which is a consequence of the electrostatic screening of attractive interactions between BSA and NaPSS. Distinct anion-specific trends were observed in which the stabilizing effect of the salt increased in the order: NaCl < NaBr < NaI. The presence of PEG, regardless of its molecular weight, showed no measurable effect on the formation of soluble complexes. PEG-400 and PEG-3000 showed no effect on the formation of insoluble complexes, but PEG-20000 in high concentrations promoted their formation due to the molecular crowding effect. The presence of sugar molecules had little effect on BSA-NaPSS complexation. Sucralose showed a minor stabilizing effect with respect to the onset of complex formation, which was due to its propensity to the protein surface. This was confirmed by the fluorescence quenching assay (Stern-Volmer relationship) and all-atom MD simulations. This study highlights that when evaluating the modulatory effect of co-solutes on protein-polyelectrolyte interactions, (co-solute)-protein interactions and their subsequent impact on protein aggregation must also be considered.https://www.mdpi.com/2073-4360/14/6/1245protein-PE complexationsolid-liquid phase separationsucrosesucralosemolecular crowdingelectrostatic screening |
| spellingShingle | Matjaž Simončič Miha Lukšič Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate Polymers protein-PE complexation solid-liquid phase separation sucrose sucralose molecular crowding electrostatic screening |
| title | Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate |
| title_full | Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate |
| title_fullStr | Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate |
| title_full_unstemmed | Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate |
| title_short | Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate |
| title_sort | modulating role of co solutes in complexation between bovine serum albumin and sodium polystyrene sulfonate |
| topic | protein-PE complexation solid-liquid phase separation sucrose sucralose molecular crowding electrostatic screening |
| url | https://www.mdpi.com/2073-4360/14/6/1245 |
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