- Protease inhibitors from a water bloom of the cyanobacterium Microcystis aeruginosa
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Bioassay-guided fractionation of the polar extract of a Microcystis aeruginosa water bloom biomass yielded 10 micropeptins and one anabaenopeptin. Eight of the micropeptins, micropeptins HU1069 (1), HU989 (2), HU1021 (3), HU1041 (4), HU975 (5), HU895A (6)
- Gesner-Apter, Shiri,Carmeli, Shmuel
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- Streptobactin, a tricatechol-type siderophore from marine-derived streptomyces sp. YM5-799
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A new catechol-type siderophore, streptobactin (1), was isolated from a culture broth of the marine-derived actinomycete Streptomyces sp. YM5-799. The structure of streptobactin was determined by NMR and MS analyses and ESIMS/MS experiments to be a cyclic trimer of benarthin. A dibenarthin (2), a tribenarthin (3), and benarthin (4) were also obtained. The production of 1 was regulated by an iron concentration in the culture. The iron-chelating activity of the compounds was evaluated by the chrome azurol sulfonate assay.
- Matsuo, Yoshihide,Kanoh, Kaneo,Jang, Jae-Hyuk,Adachi, Kyoko,Matsuda, Satoru,Miki, Osamu,Kato, Toshiaki,Shizuri, Yoshikazu
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- Ruckerbactin Produced by Yersinia ruckeri YRB Is a Diastereomer of the Siderophore Trivanchrobactin Produced by Vibrio campbellii DS40M4
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The Gram-negative bacterium Yersinia ruckeri is the causative agent for enteric red mouth disease in salmonids. The genome of Y. ruckeri YRB contains a biosynthetic gene cluster encoding the biosynthesis of catechol siderophores that are diastereomeric with the known vanchrobactin class of siderophores, (DHBDArgLSer)(1–3). Ruckerbactin (1), produced by Y. ruckeri YRB, was found to be the linear tris-l-serine ester composed of l-arginine and 2,3-dihydroxybenzoic acid, (DHBLArgLSer)3. The biscatechol, (DHBLArgLSer)2 (2), and monocatechol, DHBLArgLSer (3), compounds were also isolated and characterized. The macrolactone of ruckerbactin was not detected. The presence of LArg in ruckerbactin makes it the diastereomer of trivanchrobactin with DArg. The electronic circular dichroism spectra of Fe(III)–ruckerbactin and Fe(III)–trivanchrobactin reveal the opposite enantiomeric configurations at the Fe(III) sites. Fe(III)–ruckerbactin adopts the Δ configuration, and Fe(III)–trivanchrobactin adopts the Λ configuration. Y. ruckeri YRB was also found to produce the antimicrobial agent holomycin (4).
- Butler, Alison,Dulaney, Kalana,Reitz, Zachary L.,Stow, Parker R.,Thomsen, Emil
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p. 264 - 269
(2022/01/15)
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- Namalides B and C and Spumigins K-N from the Cultured Freshwater Cyanobacterium Sphaerospermopsis torques-reginae
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Chemical investigations of the terrestrial cyanobacterium Sphaerospermopsis torques-reginae ITEP-024 from northern Brazil afforded namalides B (1) and C (2), the first analogues of this anabaenopeptide-like metabolite to be described. Four other related peptides (3-6), termed spumigins K-N, were also identified. Planar structures and absolute configurations for 1, 2, and 3a-6a were deduced by a combination of 2D NMR, HRMS analysis, and Marfey's methodology. Spumigins K-N (3-6) are the first examples of spumigins containing a 2-hydroxy-4-(4-hydroxyphenyl)butanoic acid (Hhpba) in the N-terminal position. Compounds 1 and 2 inhibited carboxypeptidase A with IC50 values of 0.75 and 2.0 μM, respectively.
- Sanz, Miriam,Salinas, Roberto Kopke,Pinto, Ernani
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p. 2492 - 2501
(2017/09/27)
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- C3 and 2D C3 Marfey's Methods for Amino Acid Analysis in Natural Products
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We validate the improved resolution and sensitivity of the C3 Marfey's method, including an ability to resolve all Ile isomers, against an array of amino acids commonly encountered in natural products and by comparison to an existing Marfey's m
- Vijayasarathy, Soumini,Prasad, Pritesh,Fremlin, Leith J.,Ratnayake, Ranjala,Salim, Angela A.,Khalil, Zeinab,Capon, Robert J.
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supporting information
p. 421 - 427
(2016/03/05)
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- Eight micropeptins from a Microcystis spp. bloom collected from a fishpond near Kibbutz Lehavot HaBashan, Israel
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Eight new micropeptin-type cyclic depsipeptides, micropeptins LH920, LH1021, LH1048, LH1062, LH911A, LH911B, LH911C, and LH925, along with five known micropeptins, three known anabaenopeptins and two known microcystins (LR and RR), were isolated from a wa
- Vegman, Margarita,Carmeli, Shmuel
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p. 10108 - 10115
(2013/11/06)
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- Protease inhibitors from microcystis aeruginosa bloom material collected from the dalton reservoir, israel
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Nine new metabolites, aeruginosins DA495A (1), DA511 (2), DA642A (3), DA642B (4), DA688 (5), DA722 (6), and DA495B (7), microguanidine DA368 (8), and anabaenopeptin DA850 (9), were isolated along with the known micropeptins MZ924, MZ939A, and MZ1019, cyanopeptolins S and SS, microcin SF608, and aeruginazoles DA1497, DA1304, and DA1274 from bloom material of the cyanobacterium Microcystis aeruginosa collected from the Dalton reservoir, Israel, in October 2007. Their structures were elucidated by a combination of various spectroscopic techniques, primarily NMR and MS, while the absolute configurations of the asymmetric centers were determined by Marfey's and chiral-phase HPLC methods. Two of the new aeruginosins, DA511 (1) and DA495A (2), contain a new Choi isomer, (2S,3aS,6S,7aS)-Choi. The structure elucidation and biological activities of the new metabolites are described.
- Adiv, Simi,Carmeli, Shmuel
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p. 2307 - 2315
(2014/01/17)
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- Eight novel serine proteases inhibitors from a water bloom of the cyanobacterium Microcystis sp.
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Eight new secondary metabolites, micropeptin MM836 (1), micropeptin MM850 (2), micropeptin MM916 (3), micropeptin MM932 (4), micropeptin MM978 (5), anabaenopeptin MM823 (6), anabaenopeptin MM850 (7), and anabaenopeptin MM913 (8), as well as the known anabaenopeptin B (9) were isolated from the hydrophilic extract of the cyanobacterium Microcystis sp. that was collected from a fishpond in Kibbutz Ma'agan Michael, Israel, in September 2006. The structure of the pure natural products was established by spectroscopic methods including 1D and 2D NMR, UV, 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 against the serine proteases, trypsin, chymotrypsin, thrombin and elastase.
- Zafrir-Ilan, Ella,Carmeli, Shmuel
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experimental part
p. 9194 - 9202
(2011/02/22)
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- Micropeptins from an Israeli fishpond water bloom of the cyanobacterium microcystis sp
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Seven new natural products, micropeptin MZ845 (1), micropeptin MZ859 (2), micropeptin MZ939A (3), micropeptin MZ925 (4), micropeptin MZ939B (5), micropeptin MZ1019 (6), and micropeptin MZ771 (7), as well as two known micropeptins, cyanopeptolin S (8) and cyanopeptolin SS (9), were isolated from the hydrophilic extract of the cyanobacterium Microcystis sp. that was collected from a fishpond in Kibbutz Ma'ayan Tzvi, Israel, in July 2006. 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 for HPLC. The inhibitory activity of the compounds was determined for the serine proteases: trypsin, chymotrypsin, thrombin, and elastase. These micropeptins inhibited trypsin with IC50's that varied between 0.6 and 24.2 μM. The SAR of these micropeptins is discussed.
- Zafrir, Ella,Carmeli, Shmuel
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experimental part
p. 352 - 358
(2010/08/05)
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