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Zeolite Nanoparticles for Selective Sorption of Plasma Proteins.

Rahimi M, Ng EP, Bakhtiari K, Vinciguerra M, Ali Ahmad H, Awala H, Mintova S, Daghighi M, Bakhshandeh Rostami F, de Vries M, Motazacker MM, Peppelenbosch MP, Mahmoudi M, Rezaee F - Sci Rep (2015)

Bottom Line: While the zeolite nanoparticles exposed to low plasma concentration (10%) exhibited a high selective adsorption for immunoglobulin gamma (i.e. IGHG1, IGHG2 and IGHG4) proteins.The zeolite nanoparticles can potentially be used for selectively capture of APOC-III in order to reduce the activation of lipoprotein lipase inhibition during hypertriglyceridemia treatment.The zeolite nanoparticles can be adapted to hemophilic patients (hemophilia A (F-VIII deficient) and hemophilia B (F-IX deficient)) with a risk of bleeding, and thus might be potentially used in combination with the existing therapy.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Science, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.

ABSTRACT
The affinity of zeolite nanoparticles (diameter of 8-12 nm) possessing high surface area and high pore volume towards human plasma proteins has been investigated. The protein composition (corona) of zeolite nanoparticles has been shown to be more dependent on the plasma protein concentrations and the type of zeolites than zeolite nanoparticles concentration. The number of proteins present in the corona of zeolite nanoparticles at 100% plasma (in vivo state) is less than with 10% plasma exposure. This could be due to a competition between the proteins to occupy the corona of the zeolite nanoparticles. Moreover, a high selective adsorption for apolipoprotein C-III (APOC-III) and fibrinogen on the zeolite nanoparticles at high plasma concentration (100%) was observed. While the zeolite nanoparticles exposed to low plasma concentration (10%) exhibited a high selective adsorption for immunoglobulin gamma (i.e. IGHG1, IGHG2 and IGHG4) proteins. The zeolite nanoparticles can potentially be used for selectively capture of APOC-III in order to reduce the activation of lipoprotein lipase inhibition during hypertriglyceridemia treatment. The zeolite nanoparticles can be adapted to hemophilic patients (hemophilia A (F-VIII deficient) and hemophilia B (F-IX deficient)) with a risk of bleeding, and thus might be potentially used in combination with the existing therapy.

No MeSH data available.


Related in: MedlinePlus

(a) Crystal structure of fibrinogen (crystal structure was used from PDB entry 3GHG), (b) schematic diagram of fibrinogen structure showing the flexibility of positively charged αC-domain. The amino acid sequence of αC-domain, amino acid residues 392–610, is shown below the diagram.
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f6: (a) Crystal structure of fibrinogen (crystal structure was used from PDB entry 3GHG), (b) schematic diagram of fibrinogen structure showing the flexibility of positively charged αC-domain. The amino acid sequence of αC-domain, amino acid residues 392–610, is shown below the diagram.

Mentions: The APOC-III is adsorbed on the surface of both EMT- and FAU-zeolite nanoparticles (Figure S2). The positively charged amino acid residues of APOC-III and the negatively charged EMT- and FAU-zeolite nanoparticles facilitate the electrostatic interactions and thus the adsorption of APOC-III on the zeolite surfaces. Fibrinogen is a bipolar molecule with negatively charged E and D domains, and positively charged αC-domain (PDB entry: 3GHG; Figure 6a). The αC-domain of fibrinogen Aα-chain (starts from amino acid 392 to 610) is highly flexible, mobile and positively charged31323334. This region shows positive electrostatic character, which is potentially responsible for the interaction between the fibrinogen and the negatively charged EMT- and FAU-zeolite nanoparticles. A schematic diagram of human fibrinogen structure and a flexible αC-domain of the fibrinogen are depicted in Figure 6b.


Zeolite Nanoparticles for Selective Sorption of Plasma Proteins.

Rahimi M, Ng EP, Bakhtiari K, Vinciguerra M, Ali Ahmad H, Awala H, Mintova S, Daghighi M, Bakhshandeh Rostami F, de Vries M, Motazacker MM, Peppelenbosch MP, Mahmoudi M, Rezaee F - Sci Rep (2015)

(a) Crystal structure of fibrinogen (crystal structure was used from PDB entry 3GHG), (b) schematic diagram of fibrinogen structure showing the flexibility of positively charged αC-domain. The amino acid sequence of αC-domain, amino acid residues 392–610, is shown below the diagram.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663482&req=5

f6: (a) Crystal structure of fibrinogen (crystal structure was used from PDB entry 3GHG), (b) schematic diagram of fibrinogen structure showing the flexibility of positively charged αC-domain. The amino acid sequence of αC-domain, amino acid residues 392–610, is shown below the diagram.
Mentions: The APOC-III is adsorbed on the surface of both EMT- and FAU-zeolite nanoparticles (Figure S2). The positively charged amino acid residues of APOC-III and the negatively charged EMT- and FAU-zeolite nanoparticles facilitate the electrostatic interactions and thus the adsorption of APOC-III on the zeolite surfaces. Fibrinogen is a bipolar molecule with negatively charged E and D domains, and positively charged αC-domain (PDB entry: 3GHG; Figure 6a). The αC-domain of fibrinogen Aα-chain (starts from amino acid 392 to 610) is highly flexible, mobile and positively charged31323334. This region shows positive electrostatic character, which is potentially responsible for the interaction between the fibrinogen and the negatively charged EMT- and FAU-zeolite nanoparticles. A schematic diagram of human fibrinogen structure and a flexible αC-domain of the fibrinogen are depicted in Figure 6b.

Bottom Line: While the zeolite nanoparticles exposed to low plasma concentration (10%) exhibited a high selective adsorption for immunoglobulin gamma (i.e. IGHG1, IGHG2 and IGHG4) proteins.The zeolite nanoparticles can potentially be used for selectively capture of APOC-III in order to reduce the activation of lipoprotein lipase inhibition during hypertriglyceridemia treatment.The zeolite nanoparticles can be adapted to hemophilic patients (hemophilia A (F-VIII deficient) and hemophilia B (F-IX deficient)) with a risk of bleeding, and thus might be potentially used in combination with the existing therapy.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Science, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.

ABSTRACT
The affinity of zeolite nanoparticles (diameter of 8-12 nm) possessing high surface area and high pore volume towards human plasma proteins has been investigated. The protein composition (corona) of zeolite nanoparticles has been shown to be more dependent on the plasma protein concentrations and the type of zeolites than zeolite nanoparticles concentration. The number of proteins present in the corona of zeolite nanoparticles at 100% plasma (in vivo state) is less than with 10% plasma exposure. This could be due to a competition between the proteins to occupy the corona of the zeolite nanoparticles. Moreover, a high selective adsorption for apolipoprotein C-III (APOC-III) and fibrinogen on the zeolite nanoparticles at high plasma concentration (100%) was observed. While the zeolite nanoparticles exposed to low plasma concentration (10%) exhibited a high selective adsorption for immunoglobulin gamma (i.e. IGHG1, IGHG2 and IGHG4) proteins. The zeolite nanoparticles can potentially be used for selectively capture of APOC-III in order to reduce the activation of lipoprotein lipase inhibition during hypertriglyceridemia treatment. The zeolite nanoparticles can be adapted to hemophilic patients (hemophilia A (F-VIII deficient) and hemophilia B (F-IX deficient)) with a risk of bleeding, and thus might be potentially used in combination with the existing therapy.

No MeSH data available.


Related in: MedlinePlus