Monensin Sodium, USP is a naturally occurring ionophore, used as a nonhormonal growth promoter and coccidiostat. It is a polyether antibiotic with antiparasitic activity. Monensin, but also its derivatives monensin methyl ester (MME) and monensin decyl ester (MDE) are widely used in ion-selective electrodes. Monensin is used routinely to block Golgi transport.
Monensin Sodium is soluble in chloroform, methanol, and other organic solvents and slightly soluble in water.
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| Mechanism of Action |
As an ionophore, Monensin can disrupt the natural ion gradients such as Ca2+, Mg2+, K+ and Na+, and affect transmembrane ion transport. A chemical species that reversibly binds ions, an ionophore has structure consisting of a hydrophilic center and a hydrophobic part that interacts with the biological membrane. |
| Spectrum | Gram-negative bacteria |
| Eukaryotic Cell Culture Applications |
Liver microsomes were used to study the P-450 isoenzymes involved in the biotransformation of the ionophore Monensin and how it may be affected by chemotherapeutic agents. Results suggest that P-450 3A can play an important role in the oxidative metabolism of Monensin (Nebbia et al, 1999). The monovalent cationophore Monensin can interfere with vesicular transport through the Golgi apparatus, inhibiting sphingomyelin synthesis in baby hamster kidney (BHK) cells by up to 40% (Kallen et al, 1993). |
| Solubility | Soluble in chloroform, methanol, and other organic solvents. Slightly soluble in water. |
| References |
Aowicki D and Huczyński A (2013) Structure and antimicrobial properties of Monensin A and its derivatives: Summary of the achievements. Biomed Res Int. 2013:742149 PMID 23509771 Agtarap A, Chamberlin JW, Pinkerton M, Steinrauf L. (1967) The structure of Monensic acid, a new biologically active compound. J Am Chem Soc. 89(22):5737-5739 PMID 5622366 Butaye, P, Devriese LA and Haesebrouck F (2003) Antimicrobial growth promoters used in animal feed: Effects of less well known antibiotics on Gram-positive bacteria. Clin. Microbiol. Rev. 16(2): 175–188 Griffiths G, Quinn P, Warren G (1983) Dissection of the Golgi complex. I. Monensin inhibits the transport of viral membrane proteins from medial to trans Golgi cisternae in baby hamster kidney cells infected with Semliki Forest virus. J Cell Biol. 1983 Mar;96(3):835-50. PMID 6682112 Kallen KJ, Quinn P, Allan D (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. Biochim Biophys Acta. 1166(2-3):305-308 PMID 8443249 Lowicki, D and Huczyński A (2013). Structure and antimicrobial properties of Monensin A and its derivatives: Summary of the achievements. BioMed Res. Intl. 1–14. doi:10.1155/2013/742149 |