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Depsipeptide

Type of peptide

Depsipeptide

Type of peptide

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-. Many depsipeptides have both peptide and ester linkages. Elimination of the N–H group in a peptide structure results in a decrease of H-bonding capability, which is responsible for secondary structure and folding patterns of peptides, thus inducing structural deformation of the helix and β-sheet structures. 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. They are mainly found in marine and microbial natural products.

Example of a depsipeptide with 3 amide groups (highlighted <span style=&quot;color:blue;&quot;>'''blue'''</span>) and one ester group (highlighted <span style=&quot;color:green;&quot;>'''green'''</span>). R<sup>1</sup> and R<sup>3</sup> are organic groups (e. g. methyl) or a hydrogen atom found in α-hydroxycarboxylic acids. R<sup>2</sup>, R<sup>4</sup> and R<sup>5</sup> are organic groups or a hydrogen atom found in common amino acids.

Depsipeptide natural products

thumb|right|222px|[[Enterochelin]] is a depsipeptide that is an iron-transporter. Several depsipeptides have been found to exhibit anti-cancer properties.

A depsipeptide enzyme inhibitor includes romidepsin, a member of the bicyclic peptide class, a known histone deacetylase inhibitors (HDACi). It was first isolated as a fermentation product from Chromobacterium violaceum by the Fujisawa Pharmaceutical Company.

Streptogramins, specifically streptogramin B antibiotics, 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. These form a new, potential class of antibiotics known as acyldepsipeptides (ADEPs). ADEPs target and activate the casein lytic protease (ClpP) to initiate uncontrolled peptide and unfolded protein degradation, killing many Gram-positive bacteria.

Depsipeptides can be formed through a Passerini reaction.

References

References

  1. "depsipeptides".
  2. (17 June 2011). "Benzotriazole-Mediated Syntheses of Depsipeptides and Oligoesters". The Journal of Organic Chemistry.
  3. (2014). "Peptidomimetics via modifications of amino acids and peptide bonds". Chemical Society Reviews.
  4. Yasumasa Hamada. (2005). "Recent Progress of the Synthetic Studies of Biologically Active Marine Cyclic Peptides and Depsipeptides". Chem. Rev..
  5. Walsh. (1990). "Molecular Studies on Enzymes in Chorismate Metabolism and the Enterobactin Biosynthetic Pathway". [[Chemical Reviews]].
  6. (2015). "Cyclic depsipeptides as potential cancer therapeutics". Anticancer Drugs.
  7. (2007). "The First Biologically Active Synthetic Analogues of FK228, the Depsipeptide Histone Deacetylase Inhibitor". Journal of Medicinal Chemistry.
  8. (2016). "Meyler's Side Effects of Drugs".
  9. (2010). "Activity of the streptogramin antibiotic etamycin against methicillin-resistant Staphylococcus aureus". Journal of Antibiotics.
  10. K. H. Michel, R. E. Kastner (Eli Lilly and Company), US 4492650, 1985 [Chem. Abstr. 1985, 102, 130459]
  11. (1991). "Enopeptin A, a novel depsipeptide antibiotic with anti-bacteriophage activity". The Journal of Antibiotics.
  12. (2010). "Acyldepsipeptide Antibiotics Induce The Formation Of A Structured Axial Channel In ClpP: A Model For The ClpX/ClpA-Bound State Of ClpP". Chemistry & Biology.
  13. (2006). "Medicinal Chemistry Optimization of Acyldepsipeptides of the Enopeptin Class Antibiotics". ChemMedChem.
  14. (2014). "Restriction of the Conformational Dynamics of the Cyclic Acyldepsipeptide Antibiotics Improves Their Antibacterial Activity". Journal of the American Chemical Society.
  15. Li, Jie Jack. (2021). "Passerini Reaction". Springer International Publishing.
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