Based on benzoxazole and benzothiazole scaffold as an important pharmacophore, two series of 2-(aryloxymethyl) benzoxazole and benzothiazole derivatives were synthesized and their antifungal effects against eight phytopathogenic fungi were evaluated. Compounds 5a, 5b, 5h, and 5i exhibited significant antifungal activities against most of the pathogens tested. Especially 5a, 5b, 5h, 5i, 5j, and 6h inhibited the growth of F. solani with IC₅₀ of 4.34–17.61 μg/mL, which were stronger than that of the positive control, hymexazol (IC₅₀ of 38.92 μg/mL). 5h was the most potent inhibitor (IC₅₀ of 4.34 μg/mL) against F. Solani, which was about nine times more potent than hymexazol. Most of the test compounds displayed significant antifungal effects against B. cinerea (IC₅₀ of 19.92–77.41 μg/mL), among them, 5a was the best one (IC₅₀ of 19.92 μg/mL). The structure-activity relationships (SARs) were compared and analyzed. The result indicates that the electron-drawing ability and position of the substituents have a significant impact on biological activities. Furthermore, docking studies were carried out on the lipid transfer protein sec14p from S. cerevisiae, and preliminarily verified the antifungal activities. Taken together, these results provide 2-(phenoxymethyl)benzo[d]oxazole as an encouraging framework that could lead to the development of potent novel antifungal agents.

As a dimer of proanthocyanidin, proanthocyanidin B ₂ (PB ₂ ) was found to effectively attenuate postprandial blood glucose in mice after sucrose loading.

Cyanobacterial fructose–1,6/sedoheptulose‐1,7–bisphosphatase (cy–FBP/SBPase) plays a vital role in gluconeogenesis and in the photosynthetic carbon reduction pathway, and is thus a potential enzymatic target for inhibition of harmful cyanobacterial blooms. Here, we describe the crystal structure of cy–FBP/SBPase in complex with AMP and fructose‐1,6–bisphosphate (FBP). The allosteric inhibitor AMP and the substrate FBP exhibit an unusual binding mode when in complex with cy–FBP/SBPase. Binding mode analysis suggested that AMP bound to the allosteric sites near the interface across the up/down subunit pairs C1C4 and C2C3 in the center of the tetramer, while FBP binds opposite to the interface between the horizontal subunit pairs C1C2 or C3C4. We identified a series of residues important for FBP and AMP binding, and suggest formation of a disulfide linkage between Cys75 and Cys99. Further analysis indicates that cy–FBP/SBPase may be regulated through ligand binding and alteration of the structure of the enzyme complex. The interactions between ligands and cy–FBP/SBPase are different from those of ligand‐bound structures of other FBPase family members, and thus provide new insight into the molecular mechanisms of structure and catalysis of cy–FBP/SBPase. Our studies provide insight into the evolution of this enzyme family, and may help in the design of inhibitors aimed at preventing toxic cyanobacterial blooms.Database: Structural data have ben submitted to the Protein Data Bank under accession numbers 3ROJ and 3RPL.Structured digital cy-FBP/SBPase and cy-FBP/SBPase bind by x-ray crystallography (View interaction).