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K(6)[P(2)Mo(18)O(62)] as DNase-Mimetic Artificial Nucleases to Promote Extracellular Deoxyribonucleic Acid Degradation in Bacterial Biofilms
[Image: see text] In the current study, the DNase-like activity of the Dawson-type polyoxometalate K(6)[P(2)Mo(18)O(62)] was explored. The obtained findings demonstrated that K(6)[P(2)Mo(18)O(62)] could effectively cleave phosphoester bonds in the DNA model substrate (4-nitrophenyl phosphate) and re...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10515355/ https://www.ncbi.nlm.nih.gov/pubmed/37744825 http://dx.doi.org/10.1021/acsomega.3c04790 |
Sumario: | [Image: see text] In the current study, the DNase-like activity of the Dawson-type polyoxometalate K(6)[P(2)Mo(18)O(62)] was explored. The obtained findings demonstrated that K(6)[P(2)Mo(18)O(62)] could effectively cleave phosphoester bonds in the DNA model substrate (4-nitrophenyl phosphate) and result in the degradation of plasmid DNA. Moreover, the application potential of this Dawson-type polyoxometalate as a DNase-mimetic artificial enzyme to degrade extracellular DNA (eDNA) in Escherichia coli (E. coli) bacterial biofilm was explored. The results demonstrated that K(6)[P(2)Mo(18)O(62)] exhibited high cleavage ability toward eDNA secreted by E. coli and thus eradicated the bacterial biofilm. In conclusion, Dawson-type polyoxometalate K(6)[P(2)Mo(18)O(62)] possessed desirable DNase-like activity, which could serve as a bacterial biofilm eradication agent by cleaving and degrading eDNA molecules. |
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