Depsipeptide
compounds having sequences of amino and hydroxy carboxylic acid residues (usually α-amino and α-hydroxy acids), commonly but not necessarily regularly alternating

A depsipeptide is a peptide in which one or more amide, -C(O)NHR-, linkages are replaced by the corresponding ester, -C(O)OR-. Depsipeptides usually contain alternating amide and ester linkages. Elimination of an amide linkage in a peptide structure results in a decrease of H-bonding capability, which is responsible for secondary structure within peptides, thus inducing structural warping and diversity. Because of the decreased electron delocalization in esters relative to amides, depsipeptides have lower rotational barriers and therefore are quite flexible and malleable structures. They are mainly produced in nature by soil and marine sediment inhabiting bacteria.
An example of a depsipeptide drug is the anticancer agent romidepsin, a known histone deacetylase inhibitor (HDACi). It was first isolated as a fermentation product from the soil bacterium Chromobacterium violaceum by the Fujisawa Pharmaceutical Company.
Streptogramins, specifically streptogramin B, are depsipeptides that bind to the 50S subunit of bacterial ribosomes.
Etamycin was shown in preliminary data in 2010 to have potent activity against MRSA in a mouse model.
Several depsipeptides from Streptomyces exhibit antimicrobial activity.
This brief starts where responsible research should: with the source description of “Depsipeptide” as compounds having sequences of amino and hydroxy carboxylic acid residues (usually α-amino and α-hydroxy acids), commonly but not necessarily regularly alternating. Everything that follows is an evidence route, not borrowed authority.
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The subject matters to the general reference register because the source frames it as compounds having sequences of amino and hydroxy carboxylic acid residues (usually α-amino and α-hydroxy acids), commonly but not necessarily regularly alternating. Its deeper value depends on whether names, dates, institutions and citations support that framing.
Vocabulary and entity names are the principal evidence signals here, because they determine the precision of every later search. The source revision retrieved here is dated Jul 8, 2026. The linked authority identifier is Q413248. None of the 0 selected statements returned an explicit reference. The first chronological checks are 2010.
The absence of detail may reflect summary conventions rather than a lack of surviving documentation. The lead is largely declarative, so disagreement and counter-evidence require a deliberate search beyond the opening account. Authority statements aid reconciliation but still require their own references, qualifiers and ranks to be checked.
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This entry incorporates text from “Depsipeptide” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.