K6[P2Mo18O62] as DNase-Mimetic Artificial Nucleases to Promote Extracellular Deoxyribonucleic Acid Degradation in Bacterial Biofilms

Shaoling Lin; Jing Li; Feng Zhou; Bee K Tan; Baodong Zheng; Jiamiao Hu

doi:10.1021/acsomega.3c04790

K₆[P₂Mo₁₈O₆₂] as DNase-Mimetic Artificial Nucleases to Promote Extracellular Deoxyribonucleic Acid Degradation in Bacterial Biofilms

ACS Omega. 2023 Sep 4;8(37):33966-33974. doi: 10.1021/acsomega.3c04790. eCollection 2023 Sep 19.

Authors

Shaoling Lin¹, Jing Li¹, Feng Zhou¹, Bee K Tan², Baodong Zheng¹, Jiamiao Hu^{1

2}

Affiliations

¹ College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
² College of Life Sciences, University of Leicester, Leicester LE1 7RH, U.K.

Abstract

In the current study, the DNase-like activity of the Dawson-type polyoxometalate K₆[P₂Mo₁₈O₆₂] was explored. The obtained findings demonstrated that K₆[P₂Mo₁₈O₆₂] 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 K₆[P₂Mo₁₈O₆₂] exhibited high cleavage ability toward eDNA secreted by E. coli and thus eradicated the bacterial biofilm. In conclusion, Dawson-type polyoxometalate K₆[P₂Mo₁₈O₆₂] possessed desirable DNase-like activity, which could serve as a bacterial biofilm eradication agent by cleaving and degrading eDNA molecules.