Description
Monensin is a naturally occuring ionophorous antibiotic that preferentially forms complexes with monovalent cations to enable transport across lipid membranes. Through its ability to affect pH and the sodium-potassium balance of a cell, monensin can induce cell death in Gram-positive bacteria such as
Micrococcus,
Bacillus, and
Staphylococcus (MICs = 1-12.5 μg/ml), reduce proliferation of
P. falciparum and
Coccicdium protozoa, and also prevent replication of certain viruses.
Chemical Properties
LIGHT CREAM AMORPHOUS POWDER
Uses
Monensin sodium salt is used in potentiometric and spectroscopic studies of alkali metal ion complexes. Monensin (Na) is a polyether small molecule ionophore, capable of forming stable complexes to monovalent cations with specific affinity for Na+. Monensin presents a highly lipophilic scaffold around the bound ion, allowing movement of the complex through the lipid bilayer and consequent transport of the ion out of the cell. Excessive flux of ions out of the cell produces a cytotoxic effect and generates the antibiotic properties of Monensin.
Uses
Poliether antibiotic. Coccidiostat.
General Description
Monensin is a polyether ionophoric antibiotic, which is produced by
Streptomyces cinnamonensis. It is used to treat bacterial, fungal and parasitic infections. Monensin prevents the growth of colon cancer cells. It facilitates the transport of sodium and potassium ions between intracellular and extracellular spaces. Monensin prevents coccidiosis?in poultry production.
Biochem/physiol Actions
Na+ ionophore; blocks glycoprotein secretion; may induce catecholamine secretion from chromaffin cells. Useful in potentiometric and spectroscopic studies of alkali metal ion complexes.
Purification Methods
Crystallise it from EtOH/H2O [Cox et al. J Am Chem Soc 107 4297 1985].
References
Aowicki and Huczynski (2013), Structure and antimicrobial properties of monensin A and its derivatives: summary of the achievements; Res. Int. 2013 742149
Kallen et al. (1993), Monensin inhibits synthesis of plasma membrane sphingomyelin by blocking transport of ceramide through the Golgi: evidence for two sites of sphingomyelin synthesis in BHK cells; Biophys. Acta 1166 305
Boss et al. (1984), Monensin-induced swelling of Golgi apparatus cisternae mediated by a proton gradient; J. Cell. Biol. 34 1
Mollenhauer et al. (1990), Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity; Biophys. Acta 1031 225
Hafner et al. (2021), The Cardenolide Glycoside Acovenoside A Interferes with Epidermal Growth Factor Receptor Trafficking in Non-Small Cell Lung Cancer Cells; Pharmacol. 12 611657
Oh-Hashi et al. (2021), Comparative Analysis of CREB3 and CREB3L2 Protein Expression in HEK293 Cells; J. Mol. Sci. 22 2767
