latrunculin a

Latrunculin A is a naturally occurring macrolide toxin isolated from the Red Sea sponge *Latrunculia magnifica* and other marine sponges. It acts as a potent inhibitor of actin polymerization by binding monomeric G-actin in a 1:1 stoichiometry with high affinity (Kd ≈ 0.2 µM), thereby preventing the formation of F-actin filaments and disrupting microfilament organization within cells[1][2][5][6]. This disruption leads to reversible morphological changes in mammalian cells and impairs cellular processes dependent on actin dynamics such as cell division and phagocytosis[7]. Latrunculin A has been widely used as a research tool to study cytoskeletal function and is under investigation for its potential anticancer properties due to its ability to inhibit mitotic spindle formation and cell replication[1][3][4].

Other names

(+)-latrunculin A(4R)-4-[(1R,4Z,8E,10Z,12S,15R,17R)-17-hydroxy-5,12-dimethyl-3-oxo-2,16-dioxabicyclo[13.3.1]nonadeca-4,8,10-trien-17-yl]-1,3-thiazolidin-2-one76343–93–6