Cyanopeptides: A New and Nearly Inexhaustible Natural Resource for the Design and Structure-Activity Relationship Studies of New Inhibitors of Trypsin-like Serine Proteases

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Abstract:

As shown in several screenings, cyanobacteria (blue-green algae) are sources of very interesting metabolites, many of which possess significant biological activities [1]. Cyanopeptides, as a rule, metabolites of a peptidic nature, show in addition to hepato- and neurotoxic properties, a broad spectrum of biological activities, including antitumour [2], immunosuppressive [3] and antimicrobial effects [4], as well as angiotensin-converting enzyme inhibitory action [5] and cardioactive effects [6].

Many of the isolated, non-toxic compounds inhibit serine proteases, which play a central role in the human organism. Trypsin-like serine proteases (e.g. thrombin, plasmin, factor Xa, t-PA, or tryptase) are the leading factors in blood coagulation, fibrinolysis, kinin-kallikrein and complement systems as well as in inflammatory processes. Both the kinin-kallikrein and complement systems are thought to be closely related to inflammation and immune reactions. Failures of one or more of these enzymes may cause a state of imbalance between protease and antiprotease (endogenous protease inhibitors) and may lead to an excess of proteolytic activity and to the development of diseases such as thrombosis, heart failures, further thromboembolic events, asthma, multiple sclerosis and pancreatitis. The discovery and development of oral inhibitors of the above mentioned enzymes therefore presents a notable measure for improving the treatment of these disorders and remains a challenge for each medicinal chemist.

This paper reviews the low-molecular weight, serine protease inhibitory cyanopeptides published over the last decade and reports on actual efforts and developments in establishing structure-activity relationships concerning the inhibition of trypsin-like serine proteases.

Keywords: biological activities; blue-green algae; cyanobacteria; cyanopeptides; inhibitors; natural products; rational drug design; serine proteases

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/157340805774580510

Affiliations: Institute of Pharmacy, Ernst-Moritz-Arndt-University Greifswald, Friedrich-Ludwig-Jahn-Str. 17, D-17489 Greifswald, Germany.

Publication date: November 1, 2005

More about this publication?
  • Current Enzyme Inhibition aims to publish all the latest and outstanding developments in enzyme inhibition studies with regards to the mechanisms of inhibitory processes of enzymes, recognition of active sites, and the discovery of agonists and antagonists, leading to the design and development of new drugs of significant therapeutic value. Each issue contains a series of timely, in-depth reviews written by leaders in the field, covering a range of enzymes that can be exploited for drug development. Current Enzyme Inhibition is an essential journal for every pharmaceutical and medicinal chemist who wishes to have up-to-date knowledge about each and every development in the study of enzyme inhibition.
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