The identification process was carried out using a two-plate system in which control organisms were compared to cells expressing FabF antisense RNA.

The molecule they identified, platensimycin (C24H27NO7, relative molecular mass 441.47), comprises two distinct structural elements connected by an amide bond.

As confirmed by total synthesis of racemic platensimycin, its structure consists of a 3-amino-2,4-dihydroxybenzoic acid polar part linked through an amide bond to a lipophilic tetracyclic ketolide.

[11] Oxidative cleavage of the double bond of this intermediate would result in the loss of the terminal three carbons producing the C-17 tetracyclic enone acid unit.

Platensimycin works by inhibiting beta-ketoacyl syntheses I/II (FabF/B), which are involved in the production of fatty acids required for bacterial cell membranes.

It interferes with enzymes involved in the condensation steps in fatty acid biosynthesis,[12] which Gram-positive bacteria need to biosynthesise cell membranes.

Other enzymes in this pathway have similarly been proven as antibiotic targets, such as FabI, the enoyl-ACP (acyl carrier protein) reductase, which is inhibited by isoniazid and related compounds and the antiseptic agent triclosan.