Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp.

Ronny Banker; Shmuel Carmeli

doi:10.1016/S0040-4020(99)00597-9

Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp.

Ronny Banker, Shmuel Carmeli^*

^*Corresponding author for this work

School of Chemistry

Research output: Contribution to journal › Article › peer-review

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
Pages (from-to)	10835-10844
Number of pages	10
Journal	Tetrahedron
Volume	55
Issue number	35
DOIs	https://doi.org/10.1016/S0040-4020(99)00597-9
State	Published - 27 Aug 1999

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title = "Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp.",

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.",

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AB - 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.

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Inhibitors of serine proteases from a waterbloom of the cyanobacterium Microcystis sp.

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