Aim: Study of influence of low concentrations of active forms of oxygen on the ability of bacteria to form biofilms and their adhesive characteristics.
Materials And Methods: Modification of the studied properties of bacteria was performed by treatment of the bacteria with hydrogen peroxide or hydroxyl radicals at concentrations of 0.5 mM that causes death of 5 - 7% of cells and non-lethal - 0.05 and 0.005 mM. Adhesive characteristics of Escherichia coli, Staphylococcus aureus, Bacillus subtilis and Klebsiella pneumoniae bacteria were determined by using human erythrocytes. The degree of biofilm formation in plates modified by collagen from human fibroblasts was determined by the amount of bound crystal violet.
Results: A significant decrease (7 - 17%) of the adhesion of E. coli, S. aureus, K. pneumoniae to erythrocytes under the influence of hydrogen peroxide and hydroxyl radicals at the concentrations of 0.5 and 0.05 mM when compared with the control was detected. 11 - 40% stimulation of E. coli, S. aureus, K. pneumoniae biofilm formation by active forms of oxygen in all the used concentrations with simultaneous insignificant biomass growth increase was noted. Active forms of oxygen did not influence significantly the studied properties of B. subtilis.
Conclusion: Active oxygen forms have regulatory influence on the character of interaction of bacteria with surfaces colonized by them, that determines structural-functional state of microbial biocenoses.
Download full-text PDF |
Source |
---|
Nanotechnology
January 2025
Guangdong Detection Center for Microbiology, 100 Xianlie Zhong Road, Guangzhou, 510070, CHINA.
In the published article "Silver nanoparticles directly formed on natural macroporous matrix and their anti-microbial activities, Nanotechnology 18 (2007) 055605", the figure caption of Figure 8 has an error in immersion time, and the correct caption is given in this Corrigendum.
View Article and Find Full Text PDFBiomacromolecules
January 2025
School of Physics and Astronomy, University of Leeds, Leeds LS2 9JT, U.K.
Enzymes are attractive as catalysts due to their specificity and biocompatibility; however, their use in industrial and biomedical applications is limited by stability. Here, we present a facile approach for enzyme immobilization within "all-enzyme" hydrogels by forming photochemical covalent cross-links between the enzyme glucose oxidase. We demonstrate that the mechanical properties of the enzyme hydrogel can be tuned with enzyme concentration and the data suggests that the dimeric nature of glucose oxidase results in unusual gel formation behavior which suggests a degree of forced induced dimer dissociation and unfolding.
View Article and Find Full Text PDFEnviron Sci Technol
January 2025
Faculty of Environmental Science and Engineering, Kunming University of Science and Technology, Kunming 650500, China.
Pt/CeO single-atom catalysts are attractive materials for CO oxidation but normally show poor activity below 150 °C mainly due to the unicity of the originally symmetric PtO structure. In this work, a highly active and stable Pt/CeO single-site catalyst with only 0.1 wt % Pt loading, achieving a satisfied complete conversion of CO at 150 °C, can be obtained through fabricating asymmetric PtO-oxygen vacancies (O) dual-active sites induced by well-dispersed NbO clusters.
View Article and Find Full Text PDFCell Rep
January 2025
Department of Medicine and Life Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain; Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain. Electronic address:
The redox state of proteins is essential for their function and guarantees cell fitness. Peroxiredoxins protect cells against oxidative stress, maintain redox homeostasis, act as chaperones, and transmit hydrogen peroxide signals to redox regulators. Despite the profound structural and functional knowledge of peroxiredoxins action, information on how the different functions are concerted is still scarce.
View Article and Find Full Text PDFBiochemistry
January 2025
Department of Developmental Biology and Genetics, Indian Institute of Science, Bengaluru 560012, India.
Eukaryotic Initiation Factor 4 (eIF4) is a group of factors that activates mRNA for translation and recruit 43S preinitiation complex (PIC) to the mRNA 5' end, forming the 48S PIC. The eIF4 factors include mRNA 5' cap-binding protein eIF4E, ATP-dependent RNA helicase eIF4A, and scaffold protein eIF4G, which anchors eIF4A and eIF4E. Another eIF4 factor, eIF4B, stimulates the RNA helicase activity of eIF4A and facilitates mRNA recruitment.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!