Abstract
Five new protease inhibitors, micropeptins SD944 ( 1), SD979 ( 2), SD999 ( 3) and SD1002 ( 4) and microginin SD755 ( 5) were isolated along with two known inhibitors, micropeptin SF995 ( 6) and microcin SF608 ( 7), from the hydrophilic extract of Microcystis aeruginosa. The planar structure of compounds 1– 5 was determined by homonuclear and inverse-heteronuclear 2D-NMR techniques as well as high-resolution mass spectrometry. The absolute configuration of the asymmetric centers was studied using Marfey's method for HPLC. Compounds 1– 4, 6 and 7 are serine-protease inhibitors while compound 5 was found to inhibit amino-proteases.
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