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Latrunculin refers to a family of natural toxins, primarily Latrunculin A and B, isolated from the marine sponge *Latrunculia magnifica*. It is a potent inhibitor of actin polymerization, acting by binding to monomeric G-actin in a 1:1 stoichiometric ratio near the nucleotide-binding cleft. This binding prevents the incorporation of actin monomers into filaments (F-actin) and promotes the disassembly of existing filaments. Due to its high specificity and potency, latrunculin is extensively used as a research reagent in cell biology to study the role of the actin cytoskeleton in processes such as cell shape maintenance, motility, and intracellular transport. While it has been explored in preclinical models for conditions like glaucoma (to increase aqueous humor outflow), it is not currently an approved therapeutic.
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