Applications of Calorimetric Techniques in the Formation of Protein-Polyelectrolytes Complexes

Romanini, Diana; Braia, Mauricio; Porfiri, María Cecilia

doi:10.5772/54260

Cited by 4 publications

(3 citation statements)

References 27 publications

(28 reference statements)

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“…Differential scanning calorimetry is an important analytical technique that measures thermal transition temperature, ie, melting temperature, T m , and the energy (enthalpy, ∆H). Various studies have highlighted the importance of DSC in investigating the polymer‐polymer interactions during PEC formation, protein‐polyelectrolyte complex, and inclusion complexes . The formation of polymer complexes and protein‐ligand systems is usually followed by changes in enthalpy, entropy, and Gibbs free energy of the system.…”

Section: Resultsmentioning

confidence: 99%

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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Section: Resultsmentioning

confidence: 99%

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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“…Then, 6 mL glycerol solution (5% w/w) is added slowly into LM-pectin solution in water (2% w/w) and stirred on a magnetic stirrer at 150 rpm for 2 h. BSA-loaded zeolite suspension is added to the pectin-glycerol solution. The interaction between polyelectrolytes and proteins requires time to achieve a high conversion of the complex [34]. Pectin-glycerol and BSA-loaded zeolite suspension are stirred at 150 rpm and 27 ± 1 • C for 24 h in a dark medium.…”

Section: Preparation Of Bsa-loaded Hydrogelsmentioning

confidence: 99%

Pectin–Zeolite-Based Wound Dressings with Controlled Albumin Release

et al. 2022

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Hypoalbuminemia can lead to poor and delayed wound healing, while it is also associated with acute myocardial infarction, heart failure, malignancies, and COVID-19. In elective surgery, patients with low albumin have high risks of postoperative wound complications. Here, we propose a novel cost-effective wound dressing material based on low-methoxy pectin and NaA-zeolite particles with controlled albumin release properties. We focused on both albumin adsorption and release phenomena for wounds with excess exudate. Firstly, we investigated albumin dynamics and calculated electrostatic surfaces at experimental pH values in water by using molecular dynamics methods. Then, we studied in detail pectin–zeolite hydrogels with both adsorption and diffusion into membrane methods using different pH values and albumin concentrations. To understand if uploaded albumin molecules preserved their secondary conformation in different formulations, we monitored the effect of pH and albumin concentration on the conformational changes in albumin after it was released from the hydrogels by using CD-UV spectroscopy analyses. Our results indicate that at pH 6.4, BSA-containing films preserved the protein’s folded structure while the protein was being released to the external buffer solutions. In vitro wound healing assay indicated that albumin-loaded hydrogels showed no toxic effects on the fibroblast cells.

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“…6C). Although still efficient, higher concentrations of PS left some RuBisCO in the supernatants in the same way as PEI: a protein-polyelectrolyte complex with a stoichiometry below 1 is usually insoluble, while overdosed system might be soluble (Romanini et al 2013). Once again, protein removal using PS was non-specific.…”

Section: Comparison Of the Procedures Using Citrate With Those Using Polyelectrolyte Precipitation And Peg Fractionationmentioning

confidence: 99%

Recombinant N-glycosylation isoforms of Legume lectins: Production and purification from Nicotiana benthamiana leaves following RuBisCO depletion

Bellande

Lalo

Ligat

et al. 2020

Plant Physiology and Biochemistry

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An efficient purification of recombinant proteins often requires a high ratio of recombinant to host proteins. In plants, Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the most abundant leaf protein, thus strongly impacting purification yield. Here, we describe a simple and robust purification procedure for recombinant proteins based on a differential precipitation of RuBisCO. In this context, four Legume lectin domains of Arabidopsis thaliana which belong to receptor-like kinases and cell wall proteins were produced from Nicotiana benthamiana leaves. The recombinant proteins exhibit a unique lectin domain consisting of around 250 amino acid residues with several predicted N-glycosylation sites and a six His-tag at the N-terminus. After ammonium sulphate precipitation of total soluble proteins, depletion of RuBisCO was obtained using citrate and succinate buffers during the salting-in step: this depletion was pH-dependent and the presence of di-or tri-carboxylic acids was required. The depleted protein extracts were then subjected to two chromatographic steps which were used in the negative mode to submit a protein fraction enriched as much as possible in recombinant lectin domains to a third chromatographic step (immobilized metalion chromatography). Three of the Legume lectin domains were purified near to homogeneity and revealed multiple N-glycosylation isoforms, particularly those from receptor-like kinases, which were characterised using specific lectins and deglycosylation enzymes. The production and purification of recombinant lectin domains will facilitate their biochemical characterisation in the context of cell-to-cell signalling and cell wall organisation.

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Applications of Calorimetric Techniques in the Formation of Protein-Polyelectrolytes Complexes

Cited by 4 publications

References 27 publications

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

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

Pectin–Zeolite-Based Wound Dressings with Controlled Albumin Release

Recombinant N-glycosylation isoforms of Legume lectins: Production and purification from Nicotiana benthamiana leaves following RuBisCO depletion

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