Synergistic effects in the processes of protein multicomponent sorption

Demin, A. A.; Mogilevskaya, A. D.; Samsonov, G. V.

doi:10.1016/s0021-9673(96)00825-4

Cited by 7 publications

(4 citation statements)

References 4 publications

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“…They are able to promote an increased level of charge matching and strengthened hydrophobic interaction, favored by their discrepancy in size, shape, and positioning of charges. We note that previous work from other authors 24 on sequential and simultaneous sorption of protein pairs on cation exchangers has demonstrated that the choice between competition and synergism depends on the conformation of the protein molecules.…”

Section: Resultsmentioning

confidence: 71%

Mixed Protein Carriers for Modulating DNA Release

Morán

Pais

Ramalho³

et al. 2009

Langmuir

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Aqueous mixtures of oppositely charged polyelectrolytes undergo associative phase separation, resulting in coacervation, gelation, or precipitation. This phenomenon has been exploited in forming DNA gel particles by interfacial diffusion. We report here the formation of DNA gel particles by mixing solutions of double-stranded DNA with aqueous solutions containing two cationic proteins, lysozyme and protamine sulfate. The effect of the lysozyme/ protamine ratio on the degree of DNA entrapment, surface morphology, swelling-deswelling behavior, and kinetics of DNA release has been investigated. By mixing the two proteins, we obtain particles that display higher loading efficiency and loading capacity values, in comparison to those obtained in single-protein systems. Examination of the release profiles has shown that in mixed protein particles, complex, dual-stage release kinetics is obtained. The overall release profile is dependent on the lysozyme/protamine ratio. The obtained profiles, or segments of them, are accuratelly fitted using the zero-order and first-order models, and the Weibull function. Fluorescence microscopy studies have suggested that the formation of these particles is associated with the conservation of the secondary structure of DNA. This study presents a new platform for controlled release of DNA from DNA gel particles formed by interfacial diffusion.

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Section: Resultsmentioning

confidence: 71%

Mixed Protein Carriers for Modulating DNA Release

Morán

Pais

Ramalho³

et al. 2009

Langmuir

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“…Synergistic sorption mechanism leads to the situation where part of protein molecules have to interact with the sorbent modified by the other protein, and it is possible that selectivity inversion took place. For example, in the initial moment the insulin was more preferably sorbed by empty sorbent, and as the sorbent phase was being filled with proteins, selectivity inversion took place, and ribonuclease was more selectively sorbed during the final process stages (16).…”

Section: Resultsmentioning

confidence: 99%

“…In our recent studies, the previously mentioned phenomena are observed during the sorption of a protein mixture on high capacity sorbents with high concentrations of the ionogenic groups in the pH range, corresponding to maximal sorption (15)(16)(17)(18)(19). The obtained data set allows us to state that synergistic effects during the multicomponent sorption process are caused by the protein's ability to be sorbed irreversibly in the given conditions, depending on the strength of protein-sorbent interaction.…”

Section: Introductionmentioning

confidence: 96%

Bi-Langmuir Isotherms' Applicability for Description of Interaction of Ion-Exchange Sorbents with Protein Mixtures

Demin

Melenevsky

2006

Journal of Chromatographic Science

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The sorption of a protein pair on carboxylic cation exchangers with various contents of ionogenic groups is examined. The bi-Langmuir isotherm calculation is carried out from sorption data for single-component systems. It is shown that good agreement of calculated and experimental data is reached only when protein-sorbent interaction weakens because of implementation of the competitive sorption mechanism.

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“…Synergetic effects appear as the increase of protein interaction with ionexchanger in the presence of another protein [4][5][6][7][8]. Protein binds so strongly to the sorbent that no displacement by another protein is possible, and if all sorption centers are occupied the further process goes on through interprotein interaction.…”

Section: Introductionmentioning

confidence: 99%