TY - JOUR
T1 - Protease inhibitors from three fishpond water blooms of Microcystis spp.
AU - Lifshits, Marina
AU - Zafrir-Ilan, Ella
AU - Raveh, Avi
AU - Carmeli, Shmuel
N1 - Funding Information:
We thank A. Sacher and K. Shereshevsky, The Mass Spectrometry Laboratory of The Maiman Institute for Proteome Research of Tel Aviv University, for the MALDI mass spectra measurements and N. Tal, the Mass Spectrometry Facility of the School of Chemistry, Tel Aviv University, for the measurements of the HR ESI mass spectra. This research was supported by the Israel Science Foundation grants 037/02 and 776/06 .
PY - 2011/6/3
Y1 - 2011/6/3
N2 - Four new natural products, micropeptin GH979 (1), microginin GH787 (2), micropeptin HM978 (3), and micropeptin HA983 (4), as well as 10 known protease inhibitors and hepatotoxins, were isolated from the hydrophilic extract of three samples of cyanobacteria (Microcystis spp.) that were collected from fishponds in Kibbutz Giva'at Haim, Kibbutz Hama'apil, and Kibbutz Gan Shmuel. The structures of the pure natural products were elucidated using spectroscopic methods, including UV, 1D and 2D NMR, and MS techniques. The absolute configuration of the chiral centers of the compounds was determined using Marfey's method. The inhibitory activity of the compounds was determined for the serine proteases: trypsin, chymotrypsin, thrombin and elastase, and the metalloprotease, aminopeptidase N.
AB - Four new natural products, micropeptin GH979 (1), microginin GH787 (2), micropeptin HM978 (3), and micropeptin HA983 (4), as well as 10 known protease inhibitors and hepatotoxins, were isolated from the hydrophilic extract of three samples of cyanobacteria (Microcystis spp.) that were collected from fishponds in Kibbutz Giva'at Haim, Kibbutz Hama'apil, and Kibbutz Gan Shmuel. The structures of the pure natural products were elucidated using spectroscopic methods, including UV, 1D and 2D NMR, and MS techniques. The absolute configuration of the chiral centers of the compounds was determined using Marfey's method. The inhibitory activity of the compounds was determined for the serine proteases: trypsin, chymotrypsin, thrombin and elastase, and the metalloprotease, aminopeptidase N.
KW - Anabaenopeptins
KW - Cyanobacteria
KW - Microcystis
KW - Micropeptins
KW - Natural products
UR - http://www.scopus.com/inward/record.url?scp=79955833405&partnerID=8YFLogxK
U2 - 10.1016/j.tet.2011.04.042
DO - 10.1016/j.tet.2011.04.042
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AN - SCOPUS:79955833405
SN - 0040-4020
VL - 67
SP - 4017
EP - 4024
JO - Tetrahedron
JF - Tetrahedron
IS - 22
ER -