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Polyhydroxy p-Terphenyls from a Mangrove Endophytic Fungus Aspergillus candidus LDJ-5
Authors:Guoliang Zhou  Xiaomin Zhang  Mudassir Shah  Qian Che  Guojian Zhang  Qianqun Gu  Tianjiao Zhu  Dehai Li
Institution:1.Key Laboratory of Marine Drugs, Chinese Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, China; (G.Z.); (X.Z.); (M.S.); (Q.C.); (G.Z.); (Q.G.);2.Laboratory for Marine Drugs and Bioproducts, Pilot National Laboratory for Marine Science and Technology, Qingdao 266237, China;3.Open Studio for Druggability Research of Marine Natural Products, Pilot National Laboratory for Marine Science and Technology, Qingdao 266237, China
Abstract:Six undescribed polyhydroxy p-terphenyls, namely asperterphenyllins A–F, were isolated from an endophytic fungus Aspergillus candidus LDJ-5. Their structures were determined by NMR and MS data. Differing from the previously reported p-terphenyls, asperterphenyllin A represents the first p-terphenyl dimer connected by a C-C bond. Asperterphenyllin A displayed anti-influenza virus A (H1N1) activity and protein tyrosine phosphatase 1B (PTP1B) inhibitory activity with IC50 values of 53 μM and 21 μM, respectively. The anti-influenza virus A (H1N1) activity and protein tyrosine phosphatase 1B (PTP1B) inhibitory activity of p-terphenyls are reported for the first time. Asperterphenyllin G exhibited cytotoxicity against nine cell lines with IC50 values ranging from 0.4 to 1.7 μM. Asperterphenyllin C showed antimicrobial activity against Proteus species with a MIC value of 19 μg/mL.
Keywords:Aspergillus candidus  p-terphenyl dimer  anti-influenza virus A (H1N1) activity  protein tyrosine phosphatase 1B (PTP1B) inhibitory activity
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