OLIGOMYCIN A

Description

Oligomycins are macrolides created by Streptomyces species that can be toxic to other organisms. Different oligomycin isomers are highly specific for the disruption of mitochondrial metabolism. Oligomycin A, a dominant analog of the isomers, is an inhibitor of mitochondrial F₁F_O ATP synthase that induces apoptosis in a variety of cell types (average GI₅₀ = 270 nM). Oligomycin A exhibits antifungal, antitumor, and nematocidal activities, but has poor solubility in water and other biocompatible solvents, which limits its clinical application.

Chemical Properties

White powder

Uses

Oligomycin A is the dominant analogue of a class of macrocyclic lactones isolated from selected strains of Streptomyces sp.. Oligomycin A is an inhibitor of mitochondrial F1F0-ATPase. It induces apoptosis in a variety of cell types, makes cells more susceptible to cell death, and also leads to a switch in the death mode from apoptosis to necrosis. Oligomycin A exhibits a broad biological profile including antifungal, antitumor and nematocidal activities.

Uses

Oligomycin A is the dominant analogue of a class macrocyclic lactones isolated from selected strains of Streptomyces sp.. Oligomycin A is an inhibitor of mitochondrial F1F0-ATPase. It induces apoptosis in a variety of cell types, makes cells more susceptible to cell death, and also leads to a switch in the death mode from apoptosis to necrosis. Oligomycin A exhibits a broad biological profile including antifungal, antitumour and nematocidal activities.

Uses

Oligomycin A is a macrolide with fungicidal activity isolated from Streptomyces species.

storage

-20°C

References

[1]. jastroch m, divakaruni as, mookerjee s, et al. mitochondrial proton and electron leaks. essays biochemistry, 2010, 47:53-67.
[2]. shchepina la, pletjushkina oy, avetisyan av, et al. oligomycin, inhibitor of the f-0 part of h+-atp-synthase, suppresses the tnf-induced apoptosis. oncogene, 2002, 53: 8149-8157.
[3]. salomon ar, voehringer dw, herzenberg la, et al. understanding and exploiting the mechanistic basis for selectivity of polyketide inhibitors of f0f1-atpase. proceedings of the national academy of sciences of the united states of america, 2000, 97(26): 14766-14771.
[4]. alexander r, adina v, ivan b,　et al. overcoming intrinsic multi-drug resistance in melanoma by blocking the mitochondrial respiratory chain of slow-cycling jarid1bhigh cells. cancer cell, 2013, 23(6): 811-825.