Kombinatorische Chemie als Pool für neue Arzneistoffe

Radau, Gregor

doi:10.1002/pauz.19970260106

Cited by 9 publications

(19 citation statements)

References 8 publications

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“…(25). [158,159] These depsipeptides are characterized by an aminohydroxypiperidone (Ahp) unit, a N-methylated amino acid, a threonine, where the lactone ring is formed, and an attached peptidic side-chain, which is often terminated by either hydrophobic fatty acids or polar acids. Up to now, many of these depsipeptides have been isolated from cyanobacteria.…”

Section: Protease Inhibitorsmentioning

confidence: 99%

Secondary Metabolites from Cyanobacteria: Complex Structures and Powerful Bioactivities

Gademann¹,

Portmann

2008

COC

237

168

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This review presents natural products from cyanobacteria. Several classes of secondary metabolites are highlighted. Toxic metabolites from these prokaryotic photosynthetic organisms include compounds such as microcystin, anatoxin and saxitoxin, which display hepatotoxicity and neurotoxicity. Their potential as drugs in cancer therapy is discussed based on the cryptophycin class of potent cytotoxic agents. The next part of this review highlights iron chelators from cyanobacteria, including schizokinen, synechobactin and anachelin. The biogenesis of anachelin is investigated as its mechanism of iron acquisition. Several indole alkaloids are then reviewed, from simple carbolines such as bauerines and nostocarboline to complex polycyclic structures such as hapalindole, welwitindolinone and ambiguine. The latter compounds present fascinating structure combined with powerful bioactivities and interesting biogenetic pathways. In the last part, protease inhibitors from cyanobacteria are discussed (cyanopeptolins, micropeptin and oscillapeptin) and their structure/activity relationships and selectivity for trypsin / chymotrypsin are presented. All these examples highlight the large structural variety of cyanobacterial metabolites combined with powerful biological activities. Cyanobacteria can thus be considered a prime source both for novel bioactive compounds and for leads for drugs.

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Section: Protease Inhibitorsmentioning

confidence: 99%

Secondary Metabolites from Cyanobacteria: Complex Structures and Powerful Bioactivities

Gademann¹,

Portmann

2008

COC

237

168

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“…Reviews on cyanobacterial peptides having arginine or modified arginine residues, as well as other guanidine-bearing secondary metabolites, include "Serine proteases inhibiting cyanopeptides", 225 "New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria", 226 and the excellent "Production of secondary metabolites by freshwater cyanobacteria". 227 The genes encoding the biosynthesis of different cyanobacteria peptides have been sequenced and characterized, 223-237 including genes encoding the degradation of toxic peptides.…”

Section: Natural Guanidines From Terrestrial Microorganismsmentioning

confidence: 99%

“…A gene cluster that is probably responsible for the biosynthesis of onnamide A (225), originally isolated from the marine sponge Theonella swinhoei, 325 has been isolated and compared to the Paederus fuscipes beetle Pseudomonas symbiont gene cluster responsible for the biosynthesis of pederin (226). 326 It was suggested that the gene cluster isolated from T. swinhoei includes not only polyketide synthases, but also a 3-hydroxy-3-methylglutaryl-CoA synthase (HMGS), oxygenases, methyl transferases and a non-ribosomal peptide synthase (NRPS), along with genes with unidentified functions.…”

Section: Scheme 19mentioning

confidence: 99%

Natural guanidine derivatives

2005

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“…A considerable number of non-toxic cyanopeptides inhibit members of the serine proteases family [5], which play central roles in the human organism.Thus, trypsin is essential for the liberation of important pancreas enzymes, whereas trypsin-like serine proteases like thrombin, plasmin, factor Xa, t-PA, and kallikrein, represent the main actors in the interlaced cycles of blood coagulation, fibrinolysis, kinin-kallikrein system, and the complement system. A disturbance of the sensitive, by endogeneous protease inhibitors (serpins) regulated balance caused by malfunctions of one or more enzymes can result in critical effects on human organism, e.g.thromboembolic complications like venous and arterial thrombosis, stroke, restenosis, and recurrent myocardial infarction.…”

Section: Introductionmentioning

confidence: 99%

New Cyanopeptide‐Derived Low MolecularWeight Thrombin Inhibitors

Radau¹,

Gebel²,

Rauh³

2003

Archiv der Pharmazie

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Thrombosis is the result of defective regulation of the hemostasis system. This cardiovascular disorder may lead to deep vein thrombosis, myocardial infarction, and stroke. The majority of current drug research is focused on finding inhibitors of thrombin - the global player in hemostasis. In our work, we emphasize investigation of the marine environment to yield new lead structures from marine organisms like blue-green algae (cyanobacteria). This article deals with the design, syntheses, and inhibition tests of new low molecular weight thrombin inhibitors utilizing cyanopeptides, the secondary metabolites of cyanobacteria with interesting biological activities, as new lead structures. Starting with aeruginosin 98-B (2) as a lead structure, we have developed and synthesized new, selective acting inhibitors of thrombin (RA-1001 and RA-1002), which are suitable targets for further structure-activity studies.

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Kombinatorische Chemie als Pool für neue Arzneistoffe

Cited by 9 publications

References 8 publications

Secondary Metabolites from Cyanobacteria: Complex Structures and Powerful Bioactivities

Secondary Metabolites from Cyanobacteria: Complex Structures and Powerful Bioactivities

Natural guanidine derivatives

New Cyanopeptide‐Derived Low MolecularWeight Thrombin Inhibitors

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