Monensin A
Monensin A.svg
IUPAC name
4-[2-[5-Ethyl-5-[5-[6-hydroxy-6-(hydroxymethyl)-3,5-dimethyl-oxan-2-yl]-3-methyl-oxolan-2-yl]oxolan-2-yl]-9-hydroxy-2,8-dimethyl-1,6-dioxaspiro[4.5]dec-7-yl]-3-methoxy-2-methyl-pentanoic acid
Other names
Monensic acid
3D model (JSmol)
ECHA InfoCard 100.037.398
E number E714 (antibiotics)
Molar mass 670.871 g/mol
Appearance solid state, white crystals
Melting point 104 °C (219 °F; 377 K)
3x10−6 g/dm3 (20 °C)
Solubility ethanol, acetone, diethyl ether, benzene
QA16QA06 (WHO) QP51AH03 (WHO)
Related compounds
antibiotics, ionophores
Related compounds
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is ☑Y☒N ?)
Infobox references

Monensin is a polyether antibiotic isolated from Streptomyces cinnamonensis.[1] It is widely used in ruminant animal feeds.[1][2]

The structure of monensin was first described by Agtarap et al. in 1967, and was the first polyether antibiotic to have its structure elucidated in this way. The first total synthesis of monensin was reported in 1979 by Kishi et al.[3]

Mechanism of action

The structure of the sodium (Na+) complex of monensin A.

Monensin A is an ionophore related to the crown ethers with a preference to form complexes with monovalent cations such as: Li+, Na+, K+, Rb+, Ag+, and Ti+.[4][5] Monensin A is able to transport these cations across lipid membranes of cells in an electroneutral (i.e. non-depolarizing) exchange, playing an important role as an Na+/H+ antiporter. Recent studies have shown that monensin may transport sodium ion through the membrane in both electrogenic and electroneutral manner.[6] This approach explains ionophoric ability and in consequence antibacterial properties of not only parental monensin, but also its derivatives that do not possess carboxylic groups. It blocks intracellular protein transport, and exhibits antibiotic, antimalarial, and other biological activities.[7] The antibacterial properties of monensin and its derivatives are a result of their ability to transport metal cations through cellular and subcellular membranes.[8]


Monensin is used extensively in the beef and dairy industries to prevent coccidiosis, increase the production of propionic acid and prevent bloat.[9] Furthermore, monensin, but also its derivatives monensin methyl ester (MME), and particularly monensin decyl ester (MDE) are widely used in ion-selective electrodes.[10][11][12]

In laboratory research, monensin is used extensively to block Golgi transport.[13][14][15]


Monensin has some degree of activity on mammalian cells and thus toxicity is common. This is especially pronounced in horses, where monensin has a median lethal dose 1/100th that of ruminants. Accidental poisoning of equines with monensin is a well-documented occurrence which has resulted in deaths.[16]


  1. ^ a b Daniel Łowicki and Adam Huczyński (2013). "Structure and Antimicrobial Properties of Monensin A and Its Derivatives: Summary of the Achievements". BioMed Research International. 2013: 1–14. doi:10.1155/2013/742149. PMC 3586448. PMID 23509771.
  2. ^ Patrick Butaye, Luc A. Devriese, Freddy Haesebrouck "Antimicrobial Growth Promoters Used in Animal Feed: Effects of Less Well Known Antibiotics on Gram-Positive Bacteria" Clinical Microbiology Reviews, 2003, p. 175–188, Vol. 16. doi:10.1128/CMR.16.2.175-188.2003
  3. ^ Nicolaou, K. C.; E. J. Sorensen (1996). Classics in Total Synthesis. Weinheim, Germany: VCH. pp. 185–187. ISBN 3-527-29284-5.
  4. ^ Huczyński, A.; Ratajczak-Sitarz, M.; Katrusiak, A.; Brzezinski, B. (2007). "Molecular structure of the 1:1 inclusion complex of Monensin A lithium salt with acetonitrile". J. Mol. Struct. 871: 92–97. doi:10.1016/j.molstruc.2006.07.046.
  5. ^ Pinkerton, M.; Steinrauf, L. K. (1970). "Molecular structure of monovalent metal cation complexes of monensin". J. Mol. Biol. 49 (3): 533–546. doi:10.1016/0022-2836(70)90279-2.
  6. ^ Huczyński, Adam; Jan Janczak; Daniel Łowicki; Bogumil Brzezinski (2012). "Monensin A acid complexes as a model of electrogenic transport of sodium cation". Biochim. Biophys. Acta. 1818 (9): 2108–2119. doi:10.1016/j.bbamem.2012.04.017.
  7. ^ Mollenhauer, H. H.; Morre, D. J.; Rowe, L. D. (1990). "Alteration of intracellular traffic by monensin; mechanism, specificity and relationship to toxicity". Biochim. Biophys. Acta. 1031 (2): 225–246. doi:10.1016/0304-4157(90)90008-Z.
  8. ^ Huczyński, A.; Stefańska, J.; Przybylski, P.; Brzezinski, B.; Bartl, F. (2008). "Synthesis and antimicrobial properties of Monensin A esters". Bioorg. Med. Chem. Lett. 18: 2585–2589. doi:10.1016/j.bmcl.2008.03.038.
  9. ^ Matsuoka, T.; Novilla, M.N.; Thomson, T.D.; Donoho, A.L. (1996). "Review of monensin toxicosis in horses". . 16: 8–15. doi:10.1016/S0737-0806(96)80059-1.
  10. ^ K. Tohda, K. Suzuki, N. Kosuge, H. Nagashima, H. Inoue K. Watanabe, "A Sodium Ion Selective Electrode Based on a Highly Lipophilic Monensin Derivative and Its Application to the Measurement of Sodium Ion Concentrations in Serum", 6, 1990, 227–232, doi:10.2116/analsci.6.227
  11. ^ Kim, N.; Park, K.; Park, I.; Cho, Y.; Bae, Y. (2005). "Application of a taste evaluation system to the monitoring of Kimchi fermentation". Biosensors and Bioelectronics. 20: 2283–2291. doi:10.1016/j.bios.2004.10.007.
  12. ^ Toko, K. (2000). "Taste Sensor". . 64: 205–215. doi:10.1016/S0925-4005(99)00508-0.
  13. ^ Griffiths, G.; Quinn, P.; Warren, G. (March 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". The Journal of Cell Biology. 96 (3): 835–850. doi:10.1083/jcb.96.3.835. ISSN 0021-9525. PMC 2112386. PMID 6682112.
  14. ^ Kallen, K. J.; Quinn, P.; Allan, D. (1993-02-24). "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". Biochimica et Biophysica Acta. 1166 (2–3): 305–308. doi:10.1016/0005-2760(93)90111-l. ISSN 0006-3002. PMID 8443249.
  15. ^ Zhang, G. F.; Driouich, A.; Staehelin, L. A. (December 1996). "Monensin-induced redistribution of enzymes and products from Golgi stacks to swollen vesicles in plant cells". European Journal of Cell Biology. 71 (4): 332–340. ISSN 0171-9335. PMID 8980903.
  16. ^