page_title: Acyldepsipeptide antibiotics
section_title: Chemistry
hierarchical_section_title: Acyldepsipeptide antibiotics / Chemistry
caption_attribution_description: English: ADEP 1 and its synthetic congeners
context_page_description: Acyldepsipeptide or cyclic acyldepsipeptide is a class of potential antibiotics first isolated from bacteria and act by deregulating the ClpP protease. Natural ADEPs were originally found as products of aerobic fermentation in Streptomyces hawaiiensis, A54556A and B, and in the culture broth of Streptomyces species, enopeptin A and B. ADEPs are of great interest in drug development due to their antibiotic properties and thus are being modified in attempt to achieve greater antimicrobial activity.
  The potential role of ADEPs in combating antibiotic drug resistance is postulated due to their novel mode of action that other antibiotics are not known to use, activation of casein lytic protease which is an important bacterial protease. Most antibiotics work through inhibitory processes to establish cell death, while ADEPs actually work through activation of the protease to cause uncontrolled protein degradation, inhibition of cell division, and subsequent cell death.
context_section_description: ADEPs are naturally occurring antibiotics. Certain bacteria produce them as defense mechanism in antagonist bacterial interactions. For instance, Streptomyces species produce them as secondary metabolites. 
  There are 6 forms of acyl depsipeptides that are distinguishable by their chemical structure and function.  ADEPs generally differ by one or two functional groups that give some of them more flexibility, and stability. Their chemical structures are derived from ADEP 1 and are slightly different from one another. For instance, the only difference between ADEP 2 and ADEP 3 is the conformation of the difluorophenylalanine side chain. ADEP 2 has an S configuarion while ADEP 3 has an R configuarion.
caption: ADEP 1 and its synthetic congeners
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