We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties.
- Authors
Matthew, Susan; Ratnayake, Ranjala; Becerro, Mikel A.; Ritson-Williams, Raphael; Paul, Valerie J.; Luesch, Hendrik
- Abstract
Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.
- Subjects
CYANOBACTERIA; PROTEASE inhibitors; SERINE proteinases; ANTIFEEDANTS; LYNGBYA; OSCILLATORIACEAE; SEA urchins; REEF fishes; DRUGS; MARINE resources
- Publication
Marine Drugs, 2010, Vol 8, Issue 6, p1803
- ISSN
1660-3397
- Publication type
Article
- DOI
10.3390/md8061803