Abstract
Three new protease inhibitors, micropeptins SF909 (t) 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 IC50 of 4.0 μg/mL while micropeptin SF995 (2) and microcin SF608 (3) inhibited trypsin with IC50's of 0.2 and 0.5 μg/mL, respectively.
Original language | English |
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Pages (from-to) | 10835-10844 |
Number of pages | 10 |
Journal | Tetrahedron |
Volume | 55 |
Issue number | 35 |
DOIs | |
State | Published - 27 Aug 1999 |