The structure of a novel cyclic peptide (1) produced by Actinomycete sp. has been assigned on the basis of extensive NMR and mass spectral data.

In the course of screening for novel natural products, a fermentation culture broth (SCF0953) of an unidentified fungus showed strong activity in the phospholipase D (PLD) inhibitor assay. Phospholipase D is a lipolytic enzyme involved in the hydrolysis of phosphate bond of the phospholipid substrate generating phosphatidic acid. PLD activation is implicated in a wide range of biological activities such as inflammation, antitumor, and antimicrobial1^ The culture sample was described as a fungal with sterile, dematiaceous mycelium with low, dry, small blastos2). The fermentation broth was extracted with EtOAc at harvest pH (6.5). The combined extract was purified on column chromatography followed by reverse phase HPLC. The purified solid was a white powder. We

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Novel aromatic dialdehyde, Sch 207278 (1), was isolated from an unidentified fungus as an inhibitor of farnesyl protein transferase (FPTase). The structure of 1 was elucidated by spectroscopic methods. Compound 1 exhibited an IC50 value of 3.5 mu M against FPTase and 70 mu M against geranylgeranyl protein transferase-1 (GGPTase-1), respectively. (C) 1997 Elsevier Science Ltd.