|Jmol-3D images|| Image 1|
|Melting point||190 °C (374 °F; 463 K)|
|Solubility||Methanol, ethanol, ethyl acetate, petrol-ether, dichloromethane|
|LD50||4 mg/kg (oral, rat)|
|Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)|
|(what is: / ?)|
It is a member of the group of natural neutral ionophores because it does not have a residual charge. It consists of enantiomers D- and L-valine (Val), D-alpha-hydroxyisovaleric acid, and L-lactic acid. Structures are alternately bound via amide and ester bridges. Valinomycin is highly selective for potassium ions over sodium ions within the cell membrane. It functions as a potassium-specific transporter and facilitates the movement of potassium ions through lipid membranes "down" an electrochemical potential gradient. The stability constant K for the potassium-valinomycin complex is 106 and for the sodium-valinomycin complex only 10. This difference is important for maintaining the selectivity of valinomycin for the transport of potassium ions (and not sodium ions) in biological systems.
Valinomycin is a dodecadepsipeptide, that is, it is made of twelve alternating amino acids and esters to form a macrocyclic molecule. The twelve carbonyl groups are essential for the binding of metal ions, and also for solvation in polar solvent. The isopropyl and methyl groups are responsible for solvation in nonpolar solvents.  Along with its shape and size this molecular duality is the main reason for its binding properties. K ions must give up their water of hydration to pass through the pore. K+ ions are octahedrally coordinated in a square bipyramidal geometry by 6 carbonyl bonds from Val. In this space of 1.33 Angstrom, Na+ with its 0.95 Angstrom radius, is significantly smaller than the channel, meaning that Na+ cannot form ionic bonds with the amino acids of the pore at equivalent energy as those it gives up with the water molecules. This leads to a 10,000x selectivity for K+ ions over Na+. For polar solvents, valinomycin will mainly expose the carbonyls to the solvent and in nonpolar solvents the isopropyl groups are located predominantly on the exterior of the molecule. This conformation changes when valinomycin is bound to a potassium ion. The molecule is "locked" into a conformation with the isopropyl groups on the exterior. It is not actually locked into configuration because the size of the molecule makes it highly flexible, but the potassium ion gives some degree of coordination to the macromolecule.
Valinomycin was recently reported to be the most potent agent against severe acute respiratory-syndrome coronavirus (SARS-CoV) in infected Vero E6 cells.
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- Cammann K (1985). "Ion-selective bulk membranes as models". Top. Curr. Chem. 128: 219–258.
- Rose, M.C.; Henkens, R.W. (1974). "Stability of sodium and potassium complexes of valinomycin". BBA 372 (2): 426–435. doi:10.1016/0304-4165(74)90204-9.
- Thompson M and Krull UJ (1982). "The electroanalytical response of the bilayer lipid membrane to valinomycin: membrane cholesterol content". Anal. Chim. Acta 141: 33–47. doi:10.1016/S0003-2670(01)95308-5.
- Safiulina D, Veksler V, Zharkovsky A and Kaasik A (2006). "Loss of mitochondrial membrane potential is associated with increase in mitochondrial volume: physiological role in neurones". J. Cell. Physiol. 206 (2): 347–353. doi:10.1002/jcp.20476. PMID 16110491.
- Potassium ionophore Bulletin
- 1.File.tmp/k_potassium.pdf Potassium ionophore Bulletin]
- Chemical Safety Regulations from New Jersey Department of Health.
- Health information on Scorecard.
- Valinomycin from Fermentek.
- Pesticide Properties DataBase (PPDB) record for Valinomycin