Microdisperse Form of Immobilized Hemoglobin Modelling the Erythrocytes

Кузнецова, Н. П.; Mishaeva, R. N.; Gudkin, L. R.

doi:10.3109/10731199709118936

Cited by 2 publications

(3 citation statements)

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“…These substitutes encompass cross-linked or polymerized hemoglobin, polymer-conjugated hemoglobin, hydrogels, and liposomes entrapping hemoglobin. [30][31][32][33] The PMPA presents a novel promising strategy to obtain hemoglobin carriers. Up to now, the embedding of solely monomericproteinsintopolyelectrolytebrusheswasstudied.…”

Section: Introductionmentioning

confidence: 99%

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Adsorption of Bovine Hemoglobin onto Spherical Polyelectrolyte Brushes Monitored by Small-Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy

et al. 2007

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The adsorption of bovine hemoglobin (BHb) onto colloidal spherical polyelectrolyte brushes (SPBs) is studied by a combination of small-angle X-ray scattering (SAXS) and Fourier transform infrared spectroscopy (FTIR). The SPBs consist of a polystyrene core onto which long chains of poly(styrene sulfonic acid) are grafted. Hemoglobin is a tetrameric protein that disassembles at low pH's and high ionic strengths. The protein is embedded into the brush layer composed of strong polyacids. Thus, the protein is subjected to a pH and ionic strength that largely differs from the bulk solution. At low ionic strengths up to 650 mg of BHb per gram of SPB could be immobilized. The analysis of the particles loaded with protein by SAXS demonstrates that the protein enters deeply into the brush. A large fraction of hemoglobin is bound at the surface of the polystyrene core. We attribute this strong affinity to hydrophobic interactions between the protein and the polystyrene core. The other protein molecules are closely correlated with the polyelectrolyte chains. The secondary structure of the protein within the brush was studied by FTIR spectroscopy. The analysis revealed a significant disturbance of the secondary structure of the tetrameric protein. The content of alpha-helix is significantly lowered compared to the native conformation. Moreover, there is an increase of beta-sheet structure as compared to the native conformation. The partial loss of the structural integrity of the hydrophobic protein is due to hydrophobic interactions with the hydrophobic polystyrene core. Hydrophobic interactions with the phenyl groups of the poly(styrene sulfonate) chains influence the secondary structure as well. These findings indicate that changes of the secondary structure play a role in the uptake of hemoglobin into the poly(styrene sulfonate) brushes.

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Section: Introductionmentioning

confidence: 99%

“…To overcome these adverse effects associated with the free protein, much work has been devoted to blood substitutes based on immobilized hemoglobin. These substitutes encompass cross-linked or polymerized hemoglobin, polymer-conjugated hemoglobin, hydrogels, and liposomes entrapping hemoglobin. − …”

Section: Introductionmentioning

confidence: 99%

Adsorption of Bovine Hemoglobin onto Spherical Polyelectrolyte Brushes Monitored by Small-Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy

et al. 2007

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“…However, direct application may cause side effects, such as renal toxicity or vasoconstriction [99]. One solution is the immobilization of the protein onto suitable transport vehicles [100].…”

Section: Microscopic Visualization Of Protein-laden Spherical Polyelectrolyte Brushesmentioning

confidence: 99%

Adsorption mechanism, secondary structure and local distribution of proteins at polyelectrolyte brushes

Czeslik

Wittemann

2020

Colloid Polym Sci

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In many biomedical and biotechnological applications, proteins are immobilized at aqueous-solid interfaces. Generally, an adsorption-induced denaturation of the proteins has to be avoided, because it prevents the use of their biological activity or it might cause adverse effects in living organisms. Furthermore, control over the degree of protein adsorption including protein desorption is extremely useful. Over the recent years, polyelectrolyte brushes have been examined in terms of protein adsorption, and the majority of the studies document their biocompatible properties. Moreover, they show a variable protein affinity responding to the ionic strength of the protein solution. In this short review, selected studies are highlighted that illustrate the most significant properties of polyelectrolyte brushes as adsorbent interfacial structure for proteins.

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Microdisperse Form of Immobilized Hemoglobin Modelling the Erythrocytes

Cited by 2 publications

References 4 publications

Adsorption of Bovine Hemoglobin onto Spherical Polyelectrolyte Brushes Monitored by Small-Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy

Adsorption of Bovine Hemoglobin onto Spherical Polyelectrolyte Brushes Monitored by Small-Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy

Adsorption mechanism, secondary structure and local distribution of proteins at polyelectrolyte brushes

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