latrunculin a

Latrunculin A is a toxin isolated from the red sea sponge Latrunculia magnifica. Latrunculin A binds to actin monomers and it also inhibits polymerization of actin (Kds: 0.1, 0.4, 4.7 μM, and 0.19 μM for ATP-actin, ADP-Pi-actin, ADP-actin, and G-actin, re

Latrunculin M, a novel marine toxin, disrupts microfilament organization in cultured cells.

16-epiLatrunculin B, a stereoisomer of the actin polymerization inhibitor latrunculin B, was initially isolated from the Red Sea sponge N. magnifica. At concentrations of 5-10 µg/ml, it disrupts microfilament activity in actin disruption assays and exhibits cytotoxic effects on mouse KA31T and NIH3T3 tumor cells, with GI50 values of 1 and 4 µg/ml, respectively. Furthermore, it shows antiviral activity against herpes simplex type 1 virus, with an ED50 of 1 µg/ml.