Deciphering the effects of CeO2 nanoparticles on Escherichia coli in the presence of ferrous and sulfide ions: Physicochemical transformation-induced toxicity and detoxification mechanisms

2021 ◽  
Vol 413 ◽  
pp. 125300
Author(s):  
Guoxiang You ◽  
Yi Xu ◽  
Peifang Wang ◽  
Chao Wang ◽  
Juan Chen ◽  
...  
REAKTOR ◽  
2018 ◽  
Vol 18 (1) ◽  
pp. 22 ◽  
Author(s):  
Iis Nurhasanah ◽  
Weni Safitri ◽  
Tri Windarti ◽  
Agus Subagio

The CeO2 nanoparticles are very interesting to be studied as biomedical materials due to its unique physical and chemical properties. The non-stoichiometric properties of CeO2 play a role in the redox/catalytic processes that scavenging free radicals. These properties make CeO2 nanoparticles as being potentially antioxidant and radioprotector materials. In this paper, we report the calcination temperature effect on the antioxidant properties and  radioprotective effect of CeO2 nanoparticles synthesized by precipitation method. The CeO2 nanoparticles were synthesized by precipitation method at various calcinations temperatures (300oC – 700oC). The formation of CeO2 nanoparticles and crystallite size was analyzed using X-ray diffractometers. The DPPH method was used to investigate antioxidant properties of CeO2.  Dose Enhancement Factor (DEF) of CeO2 nanoparticles were determined by measurement of the absorbed dose of X-ray radiation (Linac 6 MV 200 MU). X-ray diffraction pattern showed formation of cubic fluorite of CeO2 nanoparticles with crystallite size in the range 9 nm-18 nm.  Calcination temperature of 500oC resulted in CeO2 nanoparticles with the best antioxidant properties and lowest DEF value. The radioprotection effect of CeO2 nanoparticles was evaluated based on Escherichia coli survival toward X-ray radiation with a dose of 2 Gy. The CeO2 nanoparticles increased Escherichia coli survival of about 24.8% order.  These results suggested that CeO2 nanoparticles may potentially be as radioprotector of X-ray Linac 6 MV. Keywords: Antioxidant, CeO2 nanoparticles, Dose Enhancement Factor (DEF), radioprotector


Author(s):  
G. Stöffler ◽  
R.W. Bald ◽  
J. Dieckhoff ◽  
H. Eckhard ◽  
R. Lührmann ◽  
...  

A central step towards an understanding of the structure and function of the Escherichia coli ribosome, a large multicomponent assembly, is the elucidation of the spatial arrangement of its 54 proteins and its three rRNA molecules. The structural organization of ribosomal components has been investigated by a number of experimental approaches. Specific antibodies directed against each of the 54 ribosomal proteins of Escherichia coli have been performed to examine antibody-subunit complexes by electron microscopy. The position of the bound antibody, specific for a particular protein, can be determined; it indicates the location of the corresponding protein on the ribosomal surface.The three-dimensional distribution of each of the 21 small subunit proteins on the ribosomal surface has been determined by immuno electron microscopy: the 21 proteins have been found exposed with altogether 43 antibody binding sites. Each one of 12 proteins showed antibody binding at remote positions on the subunit surface, indicating highly extended conformations of the proteins concerned within the 30S ribosomal subunit; the remaining proteins are, however, not necessarily globular in shape (Fig. 1).


Author(s):  
Manfred E. Bayer

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.


Author(s):  
Manfred E. Bayer

The first step in the infection of a bacterium by a virus consists of a collision between cell and bacteriophage. The presence of virus-specific receptors on the cell surface will trigger a number of events leading eventually to release of the phage nucleic acid. The execution of the various "steps" in the infection process varies from one virus-type to the other, depending on the anatomy of the virus. Small viruses like ØX 174 and MS2 adsorb directly with their capsid to the bacterial receptors, while other phages possess attachment organelles of varying complexity. In bacteriophages T3 (Fig. 1) and T7 the small conical processes of their heads point toward the adsorption site; a welldefined baseplate is attached to the head of P22; heads without baseplates are not infective.


Author(s):  
A.J. Verkleij

Freeze-fracturing splits membranes into two helves, thus allowing an examination of the membrane interior. The 5-10 rm particles visible on both monolayers are widely assumed to be proteinaceous in nature. Most membranes do not reveal impressions complementary to particles on the opposite fracture face, if the membranes are fractured under conditions without etching. Even if it is considered that shadowing, contamination or fracturing itself might obscure complementary pits', there is no satisfactory explanation why under similar physical circimstances matching halves of other membranes can be visualized. A prominent example of uncomplementarity is found in the erythrocyte manbrane. It is wall established that band 3 protein and possibly glycophorin represents these nonccmplanentary particles. On the other hand a number of membrane types show pits opposite the particles. Scme well known examples are the ";gap junction',"; tight junction, the luminal membrane of the bladder epithelial cells and the outer membrane of Escherichia coli.


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