Gramicidin

Gramicidins work as antibiotics against gram-positive bacteria like Bacillus subtilis and Staphylococcus aureus, but not well against gram-negative ones like E.

[13] In 1993, the structure of the gramicidin head-to-head dimer in micelles and lipid bilayers was determined by solution and solid-state NMR.

Their amino acid sequence is:[2] Y is L-tryptophan in gramicidin A, L-phenylalanine in B and L-tyrosine in C. X determines isoform.

2 gramicidins can also form antiparallel or parallel double helices, especially in organic solvents.

Dimers are long enough to span cellular lipid bilayers and thus function as ion channel -type of ionophores.

[15] Inorganic monovalent ions, such as potassium (K+) and sodium (Na+), can travel through these pores freely via diffusion.

[16] Gramicidins can be used as topical antibiotic medications in low doses, even though they are potentially lethal for human cells.

[3] Gramicidins are not used internally, as their significant intake may cause hemolysis and be toxic to the liver, kidney, meninges and olfactory system among other effects.

Gramicidin helices. Antiparallel (left) and parallel double helices and the helix dimer present in lipid bilayers. C and N are C- and N-terminals . [ 12 ]