scholarly journals Pre-coating with protein fractions inhibits nano-carrier aggregation in human blood plasma

RSC Advances ◽  
2016 ◽  
Vol 6 (99) ◽  
pp. 96495-96509 ◽  
Author(s):  
L. K. Müller ◽  
J. Simon ◽  
S. Schöttler ◽  
K. Landfester ◽  
V. Mailänder ◽  
...  

The change of a nanoparticles' physicochemical properties after incubation with defined protein fractions or whole human plasma was utilized for tailoring its properties regarding stability against aggregation and cellular response.

2015 ◽  
Vol 61 (2) ◽  
pp. 272-278
Author(s):  
Iu.V. Miroshnichenko ◽  
N.A. Petushkova ◽  
N.E. Moskaleva ◽  
N.B. Teryaeva ◽  
V.G. Zgoda ◽  
...  

Concentrations of 46 proteins have been determined in human blood plasma using PlasmaDeepDive™ MRM Panel ("Biognosys AG", Switzerland). 18 of them were included into the group of proteins with higher concentrations, also identified by the shotgun proteomic analysis. Based on literature data it is concluded that the PlasmaDeepDive™ MRM Panel is applicable for studies of human plasma samples for potential biomarkers of various nervous system disorders.


2017 ◽  
Author(s):  
Kenneth W. Witwer

AbstractA recent study reported that “Plant miRNAs found in human circulating system provide evidences of cross kingdom RNAi” 1. Analysis of two human blood plasma sequencing datasets was said to provide evidence for uptake of plant miRNAs into human plasma. The results were also purportedly inconsistent with contamination 1. However, a review of these data suggests that they do not support dietary xenomiR uptake, but instead confirm previous findings that detection of rare plant miRNAs in mammalian sequencing datasets is artifactual. Only one putative plant miRNA (“peu-MIR2910) in this study mapped consistently above background, and this sequence is found in a human rRNA. Several other rarer but consistently mapped plant miRNAs also have 100% or near 100% matches to human transcripts or genomic sequences, and some do not map to plant genomes at all. These misidentified “alternative miRNAs”—including MIR2910 and MIR2911—emphasize the need for rigorous filtering strategies when assessing possible xenomiRNAs.


Toxins ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 671
Author(s):  
Thomas P. Bambauer ◽  
Lea Wagmann ◽  
Armin A. Weber ◽  
Markus R. Meyer

Amatoxins are known to be one of the main causes of serious to fatal mushroom intoxication. Thorough treatment, analytical confirmation, or exclusion of amatoxin intake is crucial in the case of any suspected mushroom poisoning. Urine is often the preferred matrix due to its higher concentrations compared to other body fluids. If urine is not available, analysis of human blood plasma is a valuable alternative for assessing the severity of intoxications. The aim of this study was to develop and validate a liquid chromatography (LC)-high resolution tandem mass spectrometry (HRMS/MS) method for confirmation and quantitation of α- and β-amanitin in human plasma at subnanogram per milliliter levels. Plasma samples of humans after suspected intake of amatoxin-containing mushrooms should be analyzed and amounts of toxins compared with already published data as well as with matched urine samples. Sample preparation consisted of protein precipitation, aqueous liquid-liquid extraction, and solid-phase extraction. Full chromatographical separation of analytes was achieved using reversed-phase chromatography. Orbitrap-based MS allowed for sufficiently sensitive identification and quantification. Validation was successfully carried out, including analytical selectivity, carry-over, matrix effects, accuracy, precision, and dilution integrity. Limits of identification were 20 pg/mL and calibration ranged from 20 pg/mL to 2000 pg/mL. The method was applied to analyze nine human plasma samples that were submitted along with urine samples tested positive for amatoxins. α-Amanitin could be identified in each plasma sample at a range from 37–2890 pg/mL, and β-amanitin was found in seven plasma samples ranging from <20–7520 pg/mL. A LC-HRMS/MS method for the quantitation of amatoxins in human blood plasma at subnanogram per milliliter levels was developed, validated, and used for the analysis of plasma samples. The method provides a valuable alternative to urine analysis, allowing thorough patient treatment but also further study the toxicokinetics of amatoxins.


1972 ◽  
Vol 18 (6) ◽  
pp. 519-522 ◽  
Author(s):  
Richard C Kamm ◽  
Albert G Smith

Abstract Utilizing a simple, rapid, and inexpensive modification of a fluorometric method, we determined the normal concentrations of nucleic acids (DNA and RNA) in human blood plasma of healthy individuals. DNA concentrations (13.9 ± 3.7 mg/ liter) were in excellent agreement with those reported by other methods. However, the RNA concentrations (144 ± 22 mg/liter) we found were higher than previously reported values, possibly because ribonuclease activity is more inhibited in this fluorometric method.


Author(s):  
Iyan Sopyan ◽  
Cynthia Jaya ◽  
Driyanti Rahayu

The use of simvastatin (SV) increases along with the increasing number of patients with hyperlipidemia and cardiovascular disease risk factors. Consequently, this condition leads to the increasing need of analytical determination of SV in blood plasma. Analysis of SV in human plasma using protein precipitation method and HPLC with UV detector has not been reported. This research was purpose to find out the rapid, accurate, and valid of SV analysis method in human plasma. In this research plasma samples were treated with protein precipitation method. The analyte was then analyzed using HPLC with C18 column 250x4 mm and 5 µm of particle size, the mobile phase contained of phosphate buffer 0.01 M (pH 4.0) and acetonitrile 30:70 v/v with flow rate 1 mL/minute, and detected at 239 nm. The analysis method was validated based on some parameters, such as selectivity, accuracy, precision, repeatability, linearity, LOD, LOQ, and system suitability. The result showed selectivity represented by Rs was 2.870, repeatability by its CV less than 2%, and linearity by its coefficient correlation (r) 0.9992 for concentration range 0.08-0.32 ppm. Based on chromatogram peak area, LOD and LOQ were 0.0132 and 0.0440 ppm respectively, accuracy and precision were 86.25-89.36% and 0.66-1.81% were obtained. The result of system suitability test from retention time and chromatogram peak area showed by its CV less than 2%. The analysis method was proved to be valid for SV analysis in human plasma


2020 ◽  
Author(s):  
O.E.M. ter Beek ◽  
M.K. van Gelder ◽  
C. Lokhorst ◽  
D.H.M. Hazenbrink ◽  
B.H. Lentferink ◽  
...  

2018 ◽  
Vol 16 (1) ◽  
pp. 74-81 ◽  
Author(s):  
Olga I. Kiseleva ◽  
Elena A. Ponomarenko ◽  
Yulia A. Romashova ◽  
Ekaterina V. Poverennaya ◽  
Andrey V. Lisitsa

Background: Liquid chromatography coupled with targeted mass spectrometry underwent rapid technical evolution during last years and has become widely used technology in clinical laboratories. It offers confident specificity and sensitivity superior to those of traditional immunoassays. However, due to controversial reports on reproducibility of SRM measurements, the prospects of clinical appliance of the method are worth discussing. </P><P> Objective: The study was aimed at assessment of capabilities of SRM to achieve a thorough assembly of the human plasma proteome. </P><P> Method: We examined set of 19 human blood plasma samples to measure 100 proteins, including FDA-approved biomarkers, via SRM-assay. </P><P> Results: Out of 100 target proteins 43 proteins were confidently detected in at least two blood plasma sample runs, 36 and 21 proteins were either not detected in any run or inconsistently detected, respectively. Empiric dependences on protein detectability were derived to predict the number of biological samples required to detect with certainty a diagnostically relevant quantum of the human plasma proteome. </P><P> Conclusion: The number of samples exponentially increases with an increase in the number of protein targets, while proportionally decreasing to the logarithm of the limit of detection. Analytical sensitivity and enormous proteome heterogeneity are major bottlenecks of the human proteome exploration.


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