Virus Removal by Iron Coagulation Processes

Waterborne viruses account for 30% to 40% of infectious diarrhea, and some viruses could persevere for some months in nature and move up to 100 m in groundwater. Using filtration setups, coagulation could lessen virus charges as an efficient pre-treatment for reducing viruses. This work discusses the present-day studies on virus mitigation using coagulation in its three versions i.e., chemical coagulation (CC), enhanced coagulation, and electrocoagulation (EC), and debates the new results of virus demobilization. The complexity of viruses as bioparticles and the process of virus demobilization should be adopted, even if the contribution of permeability in virus sorption and aggregation needs to be clarified. The information about virion permeability has been evaluated by interpreting empirical electrophoretic mobility (EM). No practical measures of virion permeability exist, a clear link between permeability and virion composition and morphology has not been advanced, and the direct influence of inner virion structures on surface charge or sorption has yet to be conclusively demonstrated. CC setups utilizing zero-valent or ferrous iron could be killed by iron oxidation, possibly using EC and electrooxidation (EO) methods. The oxidants evolution in the iron oxidation method has depicted promising findings in demobilizing bacteriophage MS2, even if follow-up investigations employing an elution method are needed to secure that bacteriophage elimination is related to demobilization rather than sorption. As a perspective, we could be apt to anticipate virus conduct and determine new bacteriophage surrogates following subtle aspects such as protein structures or genome size and conformation. The present discussion’s advantages would extend far beyond an application in CC—from filtration setups to demobilization by nanoparticles to modeling virus fate and persistence in nature.

Characterization of a Novel 1Ay Gene and Its Expression Protein in Triticum urartu

High molecular weight glutenin subunit （HMW-GS） plays an important role in determining dough property and breadmaking quality, and the exploration of novel genes for HMW-GS will be crucial for quality improvement program. A gene coding the y type HMW-GS at Glu-A1 locus in Triticum urartu （AA, 2n=2×= 14） with an electrophoretic mobility similar to that of 1Dyl2, was cloned, sequenced, and heterologously expressed. This novel active lay gene FJ404595 was confirmed by structure analyses of nucleotide and deduced amino acid sequences combining with phylogenetic analysis. The open reading frame （ORF） of this gene was 1 830 bp, encoded a protein of 608 amino acid residues containing 46 hexapeptides and 14 nonapeptides, which was mostly similar to the lAy gene AM183223 at a high identity of 99.62% with the two substitutions of both leucine/proline and valine/glutamate, obviously different from the lAy gene EU984504 with 587 residues containing 44 hexapeptides and 13 nonapeptides in T. urartu. The amino acid （leucine） at 446 differed from that （proline） of all the eight compared active lAy subunits. The predicted secondary protein structure implied that this lAy subunit might also have positive impact on flour processing quality.

Application of a new SPA-SVM coupling method for QSPR study of electrophoretic mobilities of some organic and inorganic compounds

In this work, two chemometrics methods are applied for the modeling and prediction of electrophoretic mobilities of some organic and inorganic compounds. The successive projection algorithm, feature selection （SPA） strategy, is used as the descriptor selection and model development method. Then, the support vector machine （SVM） and multiple linear regression （MLR） model are utilized to construct the non-linear and linear quantitative structure-property relationship models. The results obtained using the SVM model are compared with those obtained using MLR reveal that the SVM model is of much better predictive value than the MLR one. The root-mean-square errors for the training set and the test set for the SVM model were 0.1911 and 0.2569, respectively, while by the MLR model, they were 0.4908 and 0.6494, respectively. The results show that the SVM model drastically enhances the ability of prediction in QSPR studies and is superior to the MLR model.

Surface modification of titanium dioxide for electrophoretic particles

To prepare stable electrophoretic ink(E Ink)needs color particles to be uniformly dispersed in the organic medium.Thus,t-he modification of inorganic particle surface is required.In this paper,Titanium dioxide modified by alumina has been studied.The surface composition and struc-tures of modified particles have been characterized by X-ray photoelectron spectrometer(XPS),X-ray diffractometer(XRD)and Fourier transform infrared spectrometer(FT-IR).The dispersibility and electrophoretic mobility of these particles in tetrachloroethylene(TCE)have been investigated by laser particle size analyzer,static sedimentation and elec-trophoretic instrument.Effects of temperature,pH value and stirring rate on the dispersibility and the charge property of samples have been discussed.The results indicate the settle time of modified TiO2 can last 120 h with the response time of 35 s under the optimized modifying conditions,in which temperature is 85℃-90℃,pH is 8-9 and stirring rate is 800 r·min^(−1).The dispersibility and electrophoretic mobility have been significantly improved,which means that the modified TiO2 is suitable for electrophoretic ink particles.

Structure and Function of N-Terminal Zinc Finger Domain of SARS-CoV-2 NSP2

SARS-CoV-2 has become a global pandemic threatening human health and safety.It is urgent to find effective therapeutic agents and targets with the continuous emergence of novel mutant strains.The knowledge of the molecular basis and pathogenesis of SARS-CoV-2 in host cells requires to be understood comprehensively.The unknown structure and function of nsp2 have hindered our understanding of its role in SARS-CoV-2 infection.Here,we report the crystal structure of the N-terminal of SARS-CoV-2 nsp2 to a high resolution of 1.96?.This novel structure contains three zinc fingers,belonging to the C2 H2,C4,and C2 HC types,respectively.Structure analysis suggests that nsp2 may be involved in binding nucleic acids and regulating intracellular signaling pathways.The binding to single or double-stranded nucleic acids was mainly through the large positively charged region on the surface of nsp2,and K111,K112,K113 were key residues.Our findings lay the foundation for a better understanding of the relationship between structure and function for nsp2.It is helpful to make full use of nsp2 as further research and development of antiviral targets and drug design.

Differently synthesized gold nanoparticles respond differently to functionalization with L-amino acids

The potential utility of gold nanoparticles(AuNPs)synthesized via different methods for biomedical applications vary greatly due to inherent differences in their surface properties.In the present study,we investigated the functionalization of AuNPs synthesized by chemical reduction,plant extract,and bacteria-mediated methods with 22 L-amino acids.Nanoparticles produced by bacteria-mediated(B_AuNPs)and plant-mediated(P_AuNPs)methods showed good potential,as they were able to be functionalized with six(histidine,lysine,methionine,phenylalanine,tryptophan,and tyrosine)and four(cystine,tryptophan,tyrosine,and valine)amino acids,respectively.In contrast,AuNPs produced by chemical reduction(C_AuNPs)were not found to be suitable for functionalization.Optimal functionalization conditions were found to be amino acid concentration of 20-25 mM and neutral pH(7)for P_AuNPs,whereas B_AuNPs tolerated more variable conditions.The electrophoretic mobility of P_AuNPs after functionalization indicated that these nanoparticles were less sensitive than B_AuNPs to the deviations from optimal conditions.A significant change in mobility was observed when B_AuNPs were functionalized with either methionine or tryptophan.Overall,the results of this study suggest that the suitability of the three differently synthesized AuNPs with amino acids is in the following order:B_AuNPs>P_AuNPs>C_AuNPs.