Complexation of bovine serum albumin with cationic polyelectrolytes at pH 7.40 – Formation of soluble complexes

Asimakopoulos, Theofanis; Staikos, Georgios

doi:10.1016/j.eurpolymj.2015.08.022

Cited by 6 publications

(5 citation statements)

References 28 publications

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“…Although a protein can also be considered a polyelectrolyte (polyampholite), we will use the term “polyelectrolyte” in the context of this article only in reference to NaPSS. BSA has already been investigated in regard to its interaction with cationic PEs, such as PDMDAAC [ 26 ], PDADMAC [ 27 , 28 , 29 ], PMAPTAC [ 27 , 30 ], chitosan [ 31 ], as well as anionic PEs, e.g., heparin [ 32 ], sugar beet pectin [ 33 ], poly(aspartic acid) [ 34 ], PAMPS [ 27 ] or NaPSS [ 26 , 35 , 36 ]. However, the modulation of BSA-NaPSS interactions by co-solutes has, at least to our knowledge, not been so systematically addressed.…”

Section: Introductionmentioning

confidence: 99%

Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate

Simončič

Lukšič

2022

Polymers

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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 pH parameters were extracted from the pH dependence of the solution’s turbidity: pHc corresponding to the formation of the soluble complexes, pHΦ corresponding to the formation of the insoluble complexes, and pHopt 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.

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Section: Introductionmentioning

confidence: 99%

Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate

Simončič

Lukšič

2022

Polymers

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“…It was observed from the figure that turbidity follows an order of 10:90 < 20:80 < 30:70 ̴ 40:60 > 50:50 > 60:40 > 70:30 > 80:20 > 90:10. The highest turbidity and low transmittance at ratio 30:70 and 40:60 indicated highest macroscopic phase separation as insoluble complexes . A comparison at different pH values (3.72, 5.5, and 7.13) for turbidity and transmittance value demonstrated that maximum turbidity and minimum transmittance were observed at pH 5.5.…”

Section: Resultsmentioning

confidence: 90%

Optimization of pH conditions and characterization of polyelectrolyte complexes between gellan gum and cationic guar gum

Kaur

2018

Polymers for Advanced Techs

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The present study was aimed to investigate optimum pH conditions for polyelectrolyte complexation between gellan gum (GG) and cationic guar gum (CGG). The pKa of both the polymers was determined using potentiometric titrations. The complex formation was investigated at three pH values (based upon the pKa interval of two polymers) and at different mixing ratios (ranging from 10:90 to 90:10). Zeta potential and turbidity studies elucidated the optimum pH and mixing ratio at which maximum interaction takes place between the polymers. The studies revealed neutral zeta potential, highest turbidity, and low transmittance at mixing ratio 30:70 and 40:60 (GG:CGG; pH 5.5), indicating maximum complex formation at these ratios. The percentage yield and viscosity studies of supernatant also revealed maximum interaction at these mixing ratios of polymers. The polyelectrolyte complexes (PECs) were characterized by Fourier transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), scanning electron microscopy (SEM), and for their swelling behavior in pH progression medium. The FTIR spectra confirmed formation of bonds between COO¯and -N + (CH 3 ) 3 of GG and CGG, respectively. DSC studies revealed the stability, affinity, and spontaneous nature of complexation between these polymers. The morphological changes detected through SEM studies in GG-CGG PECs exposed to different pH buffers also found to exhibit pH-dependent swelling. The FTIR spectra, DSC, SEM, and swelling studies of PECs treated with buffer pH 1.2 followed by buffer pH 7.4 suggested that PECs comprising 40:60 ratio of GG:CGG, prepared at pH 5.5, could be used to formulate a pH-sensitive drug delivery system.

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“…Also, the low q value might be due to a partial deprotonation of chitosan as a weak base (p K a = 6.2) at pH 5.8 so that weakly basic amino groups were not able to cause an additional ionization of BSA carboxyl groups and increase BSA charge as well as its ability to bind a large number of chitosan molecules, unlike other highly charged polymers. [ 7,27–29 ]…”

Section: Resultsmentioning

confidence: 99%

“…Also, the low q value might be due to a partial deproto-nation of chitosan as a weak base (pK a = 6.2) at pH 5.8 so that weakly basic amino groups were not able to cause an additional ionization of BSA carboxyl groups and increase BSA charge as well as its ability to bind a large number of chitosan molecules, unlike other highly charged polymers. [7,[27][28][29] Turbidimetry is an effective method for studying phase transitions in polymer systems, and, in particular, the conditions of formation and dissociation of water-insoluble complexes. Its application, along with other research methods, makes it possible to determine important parameters characterizing the process of complex formation.…”

Section: Zeta Potentials and Complexation Parametersmentioning

confidence: 99%

Effect of Soft Preheating of Bovine Serum Albumin on the Complexation with Oligochitosan: Structure and Conformation of BSA in the Complex

Zhuravleva

Bezrodnykh

Berezin

et al. 2023

Macromolecular Bioscience

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Phase analysis, spectroscopic, and light scattering methods are applied to investigate the peculiarities of the interaction of oligochitosan (OCHI) with native and preheated bovine serum albumin (BSA) as well as the conformational and structural changes of BSA in BSA/OCHI complex. As shown, untreated BSA binds with OCHI mainly forming soluble electrostatic nanocomplexes, with the binding causing an increase in BSA helicity without a change in the local tertiary structure and thermal stability of BSA. In contrast, soft preheating at 56 °C enhances the complexation of BSA with OCHI and slightly destabilizes the secondary and local tertiary structures of BSA within the complex particles. Preheating at 64 °C (below the irreversible stage of BSA thermodenaturation) leads to further enhancement in the complexation and formation of insoluble complexes stabilized by both Coulomb forces and hydrophobic interactions. The finding can be promising for the preparation of biodegradable BSA/chitosan‐based drug delivery systems.

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Complexation of bovine serum albumin with cationic polyelectrolytes at pH 7.40 – Formation of soluble complexes

Cited by 6 publications

References 28 publications

Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate

Modulating Role of Co-Solutes in Complexation between Bovine Serum Albumin and Sodium Polystyrene Sulfonate

Optimization of pH conditions and characterization of polyelectrolyte complexes between gellan gum and cationic guar gum

Effect of Soft Preheating of Bovine Serum Albumin on the Complexation with Oligochitosan: Structure and Conformation of BSA in the Complex

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