Depsipeptide

A depsipeptide is a peptide in which one or more of its amide, -C(O)NHR-, groups are replaced by the corresponding ester, -C(O)OR-.

[2][3] Because of decreased resonance delocalization in esters relative to amides, depsipeptides have lower rotational barriers for cis-trans isomerization and therefore they have more flexible structures than their native analogs.

It was first isolated as a fermentation product from Chromobacterium violaceum by the Fujisawa Pharmaceutical Company.

[7] Etamycin was shown in preliminary data in 2010 to have potent activity against MRSA in a mouse model.

ADEPs target and activate the casein lytic protease (ClpP) to initiate uncontrolled peptide and unfolded protein degradation, killing many Gram-positive bacteria.

Example of a depsipeptide with 3 amide groups (highlighted blue ) and one ester group (highlighted green ). R 1 and R 3 are organic groups (e. g. methyl) or a hydrogen atom found in α-hydroxycarboxylic acids. R 2 , R 4 and R 5 are organic groups or a hydrogen atom found in common amino acids.
Enterochelin is a depsipeptide that is an iron-transporter. [ 5 ]