scholarly journals The Protein Corona of PEGylated PGMA-Based Nanoparticles is Preferentially Enriched with Specific Serum Proteins of Varied Biological Function

Langmuir ◽  
2017 ◽  
Vol 33 (45) ◽  
pp. 12926-12933 ◽  
Author(s):  
Priya S. R. Naidu ◽  
Marck Norret ◽  
Nicole M. Smith ◽  
Sarah A. Dunlop ◽  
Nicolas L. Taylor ◽  
...  
Keyword(s):  
Biological Function ◽  
Serum Proteins ◽  
Protein Corona ◽  
Specific Serum

scholarly journals Multifunctional exosome-mimetics for targeted anti-glioblastoma therapy by manipulating protein corona

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Jun-Yong Wu ◽  
Yong-Jiang Li ◽  
Jiemin Wang ◽  
Xiong-Bin Hu ◽  
Si Huang ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Serum Proteins ◽  
Protein Corona ◽  
Significant Inhibition ◽  
Brain Drug Delivery ◽  
New Strategy ◽  
Penetration Ability ◽  
Tumor Drug Delivery ◽  
Targeting Ability ◽  
Tumor Area

AbstractTargeted drug delivery to the glioblastoma (GBM) overcoming blood–brain barrier (BBB) has been challenging. Exosomes are promising vehicles for brain tumor drug delivery, but the production and purification hinder its application for nanomedicine. Besides, the formation of protein corona (PC) may affect the behaviour of nanocarriers. Here, multifunctional exosomes-mimetics (EM) are developed and decorated with angiopep-2 (Ang) for enhancing GBM drug delivery by manipulating PC. Docetaxel (DTX)-loaded EM with Ang modification (DTX@Ang-EM) show less absorption of serum proteins and phagocytosis by macrophages. Ang-EM show enhanced BBB penetration ability and targeting ability to the GBM. Ang-EM-mediated delivery increase the concentration of DTX in the tumor area. The multifunctional DTX@Ang-EM exhibits significant inhibition effects on orthotopic GBM growth with reduced side effects of the chemotherapeutic. Findings from this study indicate that the developed DTX@Ang-EM provide a new strategy for targeted brain drug delivery and GBM therapy. Graphical abstract

scholarly journals PEGylation of Superparamagnetic Iron Oxide Nanoparticles with Self-Organizing Polyacrylate-PEG Brushes for Contrast Enhancement in MRI Diagnosis

Nanomaterials ◽  
2018 ◽  
Vol 8 (10) ◽  
pp. 776 ◽  
Author(s):  
Erzsébet Illés ◽  
Márta Szekeres ◽  
Ildikó Tóth ◽  
Katalin Farkas ◽  
Imre Földesi ◽  
...  
Keyword(s):  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Colloidal Stability ◽  
Serum Proteins ◽  
Electrokinetic Potential ◽  
Blood Compatibility ◽  
Superparamagnetic Iron Oxide ◽  
Protein Corona ◽  
Superparamagnetic Nanoparticles ◽  
Mri Diagnosis

For biomedical applications, superparamagnetic nanoparticles (MNPs) have to be coated with a stealth layer that provides colloidal stability in biological media, long enough persistence and circulation times for reaching the expected medical aims, and anchor sites for further attachment of bioactive agents. One of such stealth molecules designed and synthesized by us, poly(polyethylene glycol methacrylate-co-acrylic acid) referred to as P(PEGMA-AA), was demonstrated to make MNPs reasonably resistant to cell internalization, and be an excellent candidate for magnetic hyperthermia treatments in addition to possessing the necessary colloidal stability under physiological conditions (Illés et al. J. Magn. Magn. Mater. 2018, 451, 710–720). In the present work, we elaborated on the molecular background of the formation of the P(PEGMA-AA)-coated MNPs, and of their remarkable colloidal stability and salt tolerance by using potentiometric acid–base titration, adsorption isotherm determination, infrared spectroscopy (FT-IR ATR), dynamic light scattering, and electrokinetic potential determination methods. The P(PEGMA-AA)@MNPs have excellent blood compatibility as demonstrated in blood sedimentation, smears, and white blood cell viability experiments. In addition, blood serum proteins formed a protein corona, protecting the particles against aggregation (found in dynamic light scattering and electrokinetic potential measurements). Our novel particles also proved to be promising candidates for MRI diagnosis, exhibiting one of the highest values of r2 relaxivity (451 mM−1s−1) found in literature.

Optimizing Nephelometric Measurement of Specific Serum Proteins: Evaluation of Three Diluents

1974 ◽  
Vol 20 (12) ◽  
pp. 1548-1552 ◽  
Author(s):  
Lawrence M Killingsworth ◽  
Gregory J Buffone ◽  
Meena B Sonawane ◽  
Glennie C Lunsford
Keyword(s):  
Steady State ◽  
Continuous Flow ◽  
Reaction Rate ◽  
Serum Proteins ◽  
Physiological Saline ◽  
Rate Analysis ◽  
Specific Serum ◽  
State Approximation ◽  
Α2 Macroglobulin ◽  
Steady State Approximation

Abstract Three diluents were studied, to determine which is the best for the automated immunochemical measurement of specific serum proteins. Nine serum proteins (orosomucoid, α1-antitrypsin, α2-macroglobulin, haptoglobin, transferrin, C3, IgG, IgA, and IgM) were measured in physiological saline (9 g NaCI/liter), tris(hydroxymethyl)aminomethane buffer (0.01 mol/liter; pH 7.4), and physiological saline containing polyethylene glycol ("PEG 6000," 40 g/liter). Criteria were: reaction rate, analysis rate, carryover between samples, steady-state approximation, precision, and correlation with other methods. Saline containing polyethylene giycol is the best of the three diluents for use in continuous-flow nephelometric analysis of serum proteins.

The Transport of Thyroid Hormones

1983 ◽  
Vol 65 (4) ◽  
pp. 337-342 ◽  
Author(s):  
R. Hoffenberg ◽  
D. B. Ramsden
Keyword(s):  
Thyroid Hormones ◽  
Binding Proteins ◽  
Serum Proteins ◽  
High Capacity ◽  
Free Fraction ◽  
Total Serum ◽  
Free T4 ◽  
Specific Serum ◽  
Target Organs ◽  
Serum T4

1. Hormones have to be transported from their sites of synthesis to their target organs. For lipophilic hormones, such as steroids and thyroid hormones, transport is accomplished by binding to specific serum proteins, in the case of thyroxine (T4) and tri-iodothyronine (T3) to thyroxine-binding globulin (TBG) and prealbumin (PA). Normally about 70% of circulating T4 and 75–80% of T3 is bound to TBG, about 20% of T4 and 10% of T3 to PA and 10–15% of each to albumin, which has a low affinity but high capacity for both hormones [1, 2]. Apart from facilitating transport, binding to serum protein prevents excessive loss of hormone into the urine by glomerular filtration or flooding into cells, and may provide a readily available reservoir in times of need. The union between binding proteins and their ligands is reversible, so that a small proportion of hormone is non-protein-bound or ‘free’, in equilibrium with that which is protein-bound. For T4 this free fraction is normally 0.02-0.04% of the total serum T4 concentration, for T3 about 0.3% [3, 4]. 2. The major binding proteins of T4 and T3 will briefly be described and the nature of free T4 and T3 considered.

151 PROTEOMICS ANALYSIS OF PREGNANCY-SPECIFIC SERUM PROTEINS IN BOVINE

2006 ◽  
Vol 18 (2) ◽  
pp. 183 ◽  
Author(s):  
D. I. Jin ◽  
H. R. Lee ◽  
H. R. Kim ◽  
H. J. Lee ◽  
J. T. Yoon ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Early Pregnancy ◽  
Serum Proteins ◽  
Optical Resolution ◽  
Variable Region ◽  
Serum Samples ◽  
Proteomics Analysis ◽  
Specific Serum ◽  
Specific Proteins ◽  
Immunoglobulin Gamma

To identify early pregnancy-specific serum proteins in bovine, we performed proteomics analysis using blood serum samples of pregnant and non-pregnant Holstein dairy cattle Days 21 and 35 after AI. A total of eight pregnant and eight non-pregnant cattle were used for collection of the blood samples. The global proteomics approach was exploited by the use of 2-D gel electrophoresis and mass spectrometry to sort out pregnancy-specific proteins. Serum proteins within isoelectric point ranges of 4.0 to 7.0, 6.0 to 9.0, and 5.5 to 6.7 were analyzed separately by 2-D electrophoresis with three replications of each sample. The stained gels were scanned and calibrated at an optical resolution of 63.5 �m/pixel using a GS-710 imaging densitometer (Bio-Rad Laboratories, Philadelphia, PA, USA). A total of approximately 1200 spots were detected in 2-D gels stained with Coomassie-blue. In the comparison of serum samples from pregnant and non-pregnant cattle, nine pregnancy-specific spots were detected unanimously in Day 21 and Day 35 serum samples. Pregnancy-specific proteins were identified as transferrin, albumin, IgG2a heavy chain constant region, and immunoglobulin gamma heavy chain variable region by means of MALDI-TOF-MS (PerSeptive Biosystems, Framingham, MA, USA). Even though the identified spots were abundant serum proteins, their molecular weights and pI values were different from those of the main serum proteins. Most proteins identified in this analysis appeared to be related with pregnancy-specific subunits or fragments of transferrin, albumin, and IgG. One of the pregnancy-specific proteins, transferrin, is known to be related to iron transport during pregnancy. Western blot analysis using polyclonal anti-transferrin antibody revealed specific transferrin expression in the serum samples from the pregnant cattle but no detectable expression in the serum samples from the non-pregnant cattle. Our results revealed composite profiles of key proteins involved in early pregnancy and suggest the potential use of identified proteins to detect early pregnancy in bovine.

scholarly journals Protein corona formation around biocatalytic nanomotors unveiled by STORM

2021 ◽  
Author(s):  
Tania Patino ◽  
Joaquin Llacer-Wintle ◽  
Silvia Pujals ◽  
Lorenzo Albertazzi ◽  
Samuel Sánchez
Keyword(s):  
Serum Proteins ◽  
Biological Fluids ◽  
Protein Corona ◽  
General Interest ◽  
Biological Media ◽  
Enhanced Diffusion ◽  
Stochastic Optical Reconstruction Microscopy ◽  
Corona Formation ◽  
Active Nanoparticles ◽  
Optical Reconstruction

The interaction of nanoparticles with biological media is a topic of general interest for drug delivery systems and among those for active nanoparticles, also called nanomotors. Herein, we report the use of super resolu-tion microscopy, in particular stochastic optical reconstruction microscopy (STORM), to characterize the formation of protein corona around active enzyme-powered nanomotors. First, we characterize the distribu-tion and number of enzymes on nano-sized particles and characterized their motion capabilities. Then, we incubated the nanomotors with fluorescently labelled serum proteins. Interestingly, we observed a signifi-cant decrease of protein corona formation (20 %) and different composition, which was studied by a proteo-mic analysis. Moreover, motion was not hindered, as nanomotors displayed an enhanced diffusion regardless of protein corona. Elucidating how active particles interact with biological media and maintain their self-propulsion after protein corona formation will pave the way of the use these systems in complex biological fluids in biomedicine.

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