Analyzing the Interaction between Two Different Types of Nanoparticles and Serum Albumin

Cristian, Roxana Elena; Mohammad, Israa J.; Mernea, Maria; Sbarcea, G.; Trică, Bogdan; Stan, Miruna Silvia; Dinischiotu, Anca

doi:10.3390/ma12193183

Cited by 15 publications

(7 citation statements)

References 39 publications

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“…The amide I peak shifted from 1646 to 1657 cm –1 when HSA converted to HSANCs (Figure a). A similar peak shift of amide I (1645–1649 cm –1 ) was observed after the conversion of HSA into its nanoform and was in lieu with our results. Furthermore, the agarose gel electrophoresis displayed the presence of very minute free form of siRNA in the supernatant (lane 2) recovered postsynthesis of si-Bmi1@HSANCs compared with Bmi1 siRNA (lane 1) and pellet recovered (lane 3) diffusing (Figure d).…”

Section: Results and Discussionsupporting

confidence: 92%

“…21 The surface and morphological characterizations of nanocarriers were performed using scanning electron microscopy (SEM) (JOEL, JSM-IT300) and transmission electron microscopy (TEM). 23 The functional groups and the secondary structures in HSA and its nanocarriers were analyzed by a Fourier transform infrared (FTIR) spectroscopy 24 and circular dichroism (CD) spectrophotometer (JASCO, J-1500), 25 respectively. The pellets and the supernatant after nanocarrier purification along with bare siRNA were run on 4% agarose gel in 0.5× Tris borate ethylenediaminetetraacetic acid buffer at 80 V for 20 min, and siRNA encapsulation was calculated using following formula.…”

Section: Methodsmentioning

confidence: 99%

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Epigenetic Regulation of Bmi1 by Ubiquitination and Proteasomal Degradation Inhibit Bcl-2 in Acute Myeloid Leukemia

Kushwaha

Mohanbhai

Sardoiwala

et al. 2020

ACS Appl. Mater. Interfaces

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Bmi1 is associated with advanced prognosis of acute myeloid leukemia (AML), and polyethylenimine (PEI)-stabilized Bmi1 siRNA-entrapped human serum albumin (HSA) nanocarriers (PEI@HSANCs) were used to protect siRNA from degradation and also to control epigenetic regulation-based AML therapy. The nanoform increased the transfection efficiency of Bmi1 siRNA through caveolae-mediated endocytosis and enhanced Bax translocation into the mitochondria. It enhanced the caspase 3-mediated apoptosis through the Bax activation and Bcl-2 inhibition. The molecular analysis reveals the downregulation of polycomb proteins, Bmi1 and EzH2, along with inhibition of H3K27me3 and H2AK119ub1. The signaling cascade revealed downregulation of Bmi1 through ubiquitin-mediated degradation and is reversed by a proteasome inhibitor. Further mechanistic studies established a crucial role of transcription factor, C-Myb and Bmi1, as its direct targets for maintenance and progression of AML. Chromatin immunoprecipitation (ChIP) assay confirmed Bmi1 as a direct target of C-Myb as it binds to promoter sequence of Bmi1 between −235 to +43 and −111 to +43. The in vivo studies performed in the AML xenograft model evidence a decrease in the population of leukemic stem cells marker (CD45+) and an increase in the myeloid differentiating marker expression (CD11b+) in the bone marrow after the Bmi1 siRNA nanoconjugated therapy. Activation of apoptotic pathways and withdrawal of epigenetic repression through a ubiquitin proteasomal pathway potentiating a novel antileukemic therapy were established.

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Section: Results and Discussionsupporting

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Epigenetic Regulation of Bmi1 by Ubiquitination and Proteasomal Degradation Inhibit Bcl-2 in Acute Myeloid Leukemia

Kushwaha

Mohanbhai

Sardoiwala

et al. 2020

ACS Appl. Mater. Interfaces

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“…Even though there is experimental evidence that NP radius only has a modest effect on the affinity of proteins for NPs, , particle size may affect protein conformation and density on NPs, which in turn can affect the reversibility of adsorption. Studies were able to assess protein conformation on NP surfaces over time and suggested that a gradual loss of secondary or tertiary structure was occurring when proteins adsorbed on NPs. ,, Nevertheless, this change of structure does not appear to be systematically correlated with adsorption irreversibility. On one hand, Basu et al observed that structural changes of proteins adsorbed on poly(lactic- co -glycolic acid) NPs could occur without affecting the reversible nature of the adsorption process .…”

Section: Is Protein Adsorption On Nps a Reversible Or Irreversible Ph...mentioning

confidence: 99%

Scratching the Surface of the Protein Corona: Challenging Measurements and Controversies

et al. 2022

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This Review aims to provide a systematic analysis of the literature regarding ongoing debates in protein corona research. Our goal is to portray the current understanding of two fundamental and debated characteristics of the protein corona, namely, the formation of mono- or multilayers of proteins and their binding (ir)reversibility. The statistical analysis we perform reveals that these characterisitics are strongly correlated to some physicochemical factors of the NP–protein system (particle size, bulk material, protein type), whereas the technique of investigation or the type of measurement (in situ or ex situ) do not impact the results, unlike commonly assumed. Regarding the binding reversibility, the experimental design (either dilution or competition experiments) is also shown to be a key factor, probably due to nontrivial protein binding mechanisms, which could explain the paradoxical phenomena reported in the literature. Overall, we suggest that to truly predict and control the protein corona, future efforts should be directed toward the mechanistic aspects of protein adsorption.

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“…Therefore, our observed HSA dependent PS-particle transfer may be different from physiological HSA processing at the placental barrier. Nevertheless, corona associated albumin can change its conformation, which may directly influence particle transfer in our experiments [57,63]. Whether these results on 80 nm PS-particles are transferable to smaller or larger PS-particles needs to be investigated in future.…”

Section: Discussionmentioning

confidence: 84%

Plasma proteins facilitates placental transfer of polystyrene particles

et al. 2020

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Background Nanoparticles, which are exposed to biological fluids are rapidly interacting with proteins and other biomolecules forming a corona. In addition to dimension, charge and material the distinct protein corona influences the interplay of nanoparticles with tissue barriers. In this study we were focused on the impact of in situ formed human plasma protein corona on the transfer of 80 nm polystyrene nanoparticles (PS-particles) across the human placenta. To study materno-to fetal PS transfer we used the human ex vivo placental perfusion approach, which represents an intact and physiological tissue barrier. To analyze the protein corona of PS particles we performed shotgun proteomics of isolated nanoparticles before and after tissue exposure. Results Human plasma incubated with PS-particles of 80 nm and subsequent formed protein corona enhanced the transfer across the human placenta compared to PS-corona formed by bovine serum albumin and dextran which served as a control. Quantitative and qualitative changes of plasma proteins determined the changes in PS transfer across the barrier. Based on the analysis of the PS-proteome two candidate proteins, namely human albumin and immunoglobulin G were tested if these proteins may account for the enhanced PS-transfer across the placenta. Interestingly, the protein corona formed by human albumin significantly induced the transfer of PS-particles across the tissue compared to the formed IgG-corona. Conclusion In total we demonstrate the PS corona dynamically and significantly evolves upon crossing the human placenta. Thus, the initial composition of PS particles in the maternal circulation is not predictive for their transfer characteristics and performance once beyond the barrier of the placenta. The precise mechanism of these effects remains to be elucidated but highlights the importance of using well designed biological models when testing nanoparticles for biomedical applications.

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Analyzing the Interaction between Two Different Types of Nanoparticles and Serum Albumin

Cited by 15 publications

References 39 publications

Epigenetic Regulation of Bmi1 by Ubiquitination and Proteasomal Degradation Inhibit Bcl-2 in Acute Myeloid Leukemia

Epigenetic Regulation of Bmi1 by Ubiquitination and Proteasomal Degradation Inhibit Bcl-2 in Acute Myeloid Leukemia

Scratching the Surface of the Protein Corona: Challenging Measurements and Controversies

Plasma proteins facilitates placental transfer of polystyrene particles

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