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LKT Laboratories has recently added 24 new marine natural products and semisynthetic derivatives.
Brevetoxins are known to bind to site 5 of voltage-gated sodium channels in nerve cells, leading to channel activation. This leads to disruption of normal neurological processes and causes the illness clinically described as neurotoxic shellfish poisoning (NSP).1 Cyanopeptolins are cyclic non-ribosomal peptides isolated from various cyanobacteria.2 Cyanopeptolins have been reported to inhibit serine proteases such as trypsin and chymotrypsin.3 Microcystins are cyclic hybrid non-ribosomal peptide toxins isolated from various cyanobacteria.4 Microcystins inhibit eukaryotic protein phosphatases PP1 and PP2a and are selectively transported to the liver resulting in acute liver failure and tumor promotion.5 Microginins are a class of small, linear non-ribosomal peptides isolated from various cyanobacteria, primarily Microcystis aeruginosa. The microginins act as inhibitors against zinc metalloproteases such as angiotensin-converting enzyme6 and leucine aminopeptidase.7 Okadaic acid is a polyether from the dinoflagellate Prorocentrum lima that is the causative agent of diarrhetic shellfish poisoning (DSP).8 Okadaic acid acts as a non-phorbol ester type tumor promoter9 and as an inhibitor of protein phosphatases PP1 and PP2A.10
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1. (a) Edwards, R. A. et al. Mol. Brain Res. (1992) 14, 64–70; (b) Trainer, V. L. et al. Mol. Pharmacol. (1991) 40, 988–994; (c) Tsai, M. C., and Chen, M. L. Br. J. Pharmacol. (1991) 103, 1126–1128; (d) Trainer, V. L. et al. ACS Symposium Series (1990) 418, 166; (e) Baden, D. G. FASEB J. (1989) 3, 1807–1817; (f) Baden, D. G. et al. Toxicon (1988) 26, 97–103; (g) Poli, M. A. et al. Mol. Pharmaol. (1986) 30, 129–135; (h) Shimizu, Y. et al. J. Am. Chem. Soc. (1986) 108, 514–515; (i) Nakanishi, K. Toxicon (1985) 23, 473–479; (j) Baden, D. G. et al. Toxicon (1982) 19, 455–462; (k) Catterfall, . A. , and Risk, M. Mol. Pharmacol. (1981) 19, 345–348. 

2. Martin, C. et al. J. Antibiot. (1993) 46, 1550–1556.
3. (a) Weckesser, J. et al. Systemat. Appl. Microbiol. (1996) 19, 133–138; (b) Neumann, U, et al. Systemat. Appl. Microbiol. (2000) 23, 191–197; (c) Bister, B. et al. J. Nat. Prod. (2004) 67, 1755–1757; (d) Von Elert, E. et al. J. Nat. Prod. (2005) 68, 1324–1327.
4. (a) Carmichael, W. W. et al. Toxicon (1988) 26, 971–973; (b) Rinehart, K. L. et al. J. Am. Chem. Soc. (1988) 110, 8557–8558.

5. (a) MacKintosh, C. et al. FEBS Lett. (1990) 264, 187–192; (b) Chorus, I. et al. J. Toxicol. Env. Health B (2000) 3, 323–347; (c) Zurawell, R. et al. J. Toxicol. Env. Health B (2005) 8, 1–37.
6. (a) Okino, T. et al. Tetrahedron Lett. (1993) 34, 501–504; (b) Neumann, U. et al. FEMS Microbiol. Lett. (1997) 153, 475–478.
7. (a) Ishida, K. et al. Tetrahedron (1997) 53, 10281–10288; (b) Ishida, K. et al. Tetrahedron (1998) 54, 13475–13484; (c) Ishida, K. et al. Tetrahedron (2000) 56, 8643–8656; (d) Kraft, M. et al. FEBS Lett. (2006) 580, 6943–6947.
8. Yasumoto, T. et al. Tetrahedron (1985) 41, 1019–1025.
9.Suganuma, M. et al. Proc. Nat. Acad. Sci. USA (1988) 85, 1768–1771.
10. (a) Takai, A. et al. FEBS Lett. (1987) 217, 81–84; (b) Haystead, T. A. et al. Nature (1989) 337, 78–81.
