Applying natural product repurposing strategy to identify baicalein as novel caseinolytic protease P inhibitor and its application in the treatment of rice bacterial diseases.

Plant diseases caused by bacteria affect the yield of crop, greatly reduce the quality of food, and thus posing a great threat to food safety. To fill the gap that no report about ClpP inhibitor is applied in agri-food production field, engineering natural-product repurposing strategy, 55 of natural products were screened using the combination of ClpP inhibitors of Xanthomonas oryzae pv. oryzae (Xoo) screening assay and anti-Xoo activity experiment.

Discovery of new 1,2,3,4-tetrahydro-β-carboline derivatives decorated with 3-N-substituted propionyl moiety flexibly bridged-chain as reactive oxygen species inducer for efficient antibacterial treatment.

The widespread prevalence of bacterial plant diseases imposes a severe constraint on global food production and crop security. To address the growing challenge of bacterial resistance, there is an urgent demand to develop novel agrochemicals that combine high efficacy with low toxicity. In this study, a natural product modification strategy was employed to design new bactericidal candidates with an innovative cation mechanism.

DSF-inspired discovery of novel zingerone-based quorum-sensing inhibitors: an attractive tactic of fighting Xanthomonas bacterial infections.

Background: Plant bacterial diseases have precipitated a global crisis in human health and food security. In agriculture, diseases such as the rice white-leaf blight can cause considerable reduction in crop yields and, in extreme cases, complete crop failure. Therefore, there is an urgent need for novel green pesticides with innovative modes-of-action (MoAs).

Discovery of novel seven-membered ring derivatives of ONC212 as caseinolytic protease P protein activators using the ring expansion strategy: Rational design, synthesis, and antibacterial evaluation.

Caseinolytic protease P (ClpP) protein is essential for prokaryotic and eukaryotic protein homeostasis, and has emerged as a promising bactericidal target for controlling bacterial infection and evading the emergent of drug-resistance risk. As the unique bactericidal mechanism, ClpP loses its substrate specificity and undergoes uncontrolled protein hydrolysis in the presence of an activator, leading to causing bacterial death. To further expand the chemotype of ClpP activator, a series of ONC212 derivatives were synthesized using a ring expansion strategy.

Identification of novel 4-substituted 7H-pyrrolo[2,3-d]pyrimidine derivatives as new FtsZ inhibitors: Bioactivity evaluation and computational simulation.

Bacterial infections and the consequent outburst of bactericide-resistance issues are fatal menace to both global health and agricultural produce. Hence, it is crucial to explore candidate bactericides with new mechanisms of action. The filamenting temperature-sensitive mutant Z (FtsZ) protein has been recognized as a new promising and effective target for new bactericide discovery.