Micrococcin P1

Micrococcin P1 is a macrocyclic thiopeptide originally isolated from Micrococcus sp. by Su (Oxford) in 1948 and is considered the founding member of the thiopeptide antibiotic family. It was purified by Heatley and Doery but the producing strain was lost, causing a hiatus in research of this antibiotic family until the discovery of the related thiocillins in 1976. Its precise structure remained undefined until 2010 when researchers at University of British Columbia (Vancouver, BC) synthesized a substance that was spectroscopically and polarimetrically identical to the natural product.
Thiopeptides, characterized by posttranslationally formed sulfur- and nitrogen-containing heterocycles, constitute a rapidly expanding class of RiPP antibiotics (Ribosomally synthesized and postranslationally modified peptides), and they hold promise for natural product engineering. Micrococcin P1 has antibacterial, antiprotozoal, and gene-modulating activity. It shares a structure and intracellular target with Micrococcin P2 but differs only by two hydrogen atoms.
Micrococcin P1 is soluble in ethanol, methanol, DMF or DMSO.

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Background

Micrococcin P1 is an acceptor-site-specific inhibitor of ribosomal protein synthesis, preventing the growth of Gram-positive bacteria. It inhibits the elongation step of protein synthesis in mycobacteria, structural studies suggest it binds to the cleft between the 23S rRNA and L11 protein loop, thus interfering with the binding of elongation factors Tu and G, and inhibiting protein translocation.