Abstract
Three new protease inhibitors, micropeptins SF909 ( 1) and SF995 ( 2) and microcin SF608 ( 3), were isolated from the hydrophilic extract of a microcystis sp. waterbloom. The planar structure of compounds 1–3 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. Micropeptin SF909 ( 1) inhibited chymotrypsin with IC 50 of 4.0 μg/mL while micropeptin SF995 ( 2) and microcin SF608 ( 3) inhibited trypsin with IC 50's of 0.2 and 0.5 μg/mL, respectively.
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