Peptides from the Soft Coral-associated Fungus Simplicillium sp. SCSIO41209

Abstract Five new peptides, Sinulariapeptides A−E together with seven known peptides ( 6–12 ) were isolated from the soft coral associated fungus Simplicillium sp. SCSIO 41209. The structures of the new compounds and their absolute configurations were established on the basis of spectroscopic analysis including NMR, MS and ECD. All the Compounds (except sinulariapeptides B−D) were tested for the inhibitory activities of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB), and antifungal activities against five plant pathogenic fungi. Simplicilliumtides B and cyclo(L-Val-L-Pro) showed inhibitory activity with the IC 50 values of 35.0 and 25.9  μ M, sinulariapeptides A, simplicilliumtides J, verlamelins A and B exhibited potent inhibition against Colletotrichum asianum with the MIC values of range from 4.9 to 9.8  μ g/mL and simplicilliumtides J, verlamelins A and B displayed inhibition against Pyricularia oryza Cav with the MIC values in the range of 19.5–78.1  μ g/ml, respectively.