원문정보
초록
영어
Peptide deformylase (PDF) is essential for bacterial growth but not required by mammalian cells, which potentially makes it possible to identify a selective mechanism-based antibacterial agent without mammalian toxicity. In the course of our screening for PDF inhibitors from microbial resources, we discovered two novel dimeric 1,3- dihydroisobenzofurans, flavimycins A (1) and B (2), from the fermentation broth of Aspergillus flavipes F543. Their chemical structures were established by NMR and MS data analysis. Compounds 1 and 2 exist as epimeric mixtures at C-1 through fast hemiacetal−aldehyde tautomerism. Compounds 1 and 2 inhibited Staphylococcus aureus peptide deformylase with IC50 values of 35.8 and 100.1 μM, respectively. Consistent with their PDF inhibition, 1 showed two times stronger antibacterial activity than 2 on S. aureus including MRSA, with MIC values of 32−64 μg/mL.