Aplidine is a compound found in tunicates which shows promise in shrinking tumors in pancreatic, stomach, bladder, and prostate cancers. The specific marine organism is Aplidium albicans. Aplidine consists of peptide molecules. In addition to the cancers mentioned above it is also under consideration as a treatment for some types of leukemia.
CAT No: 10-101-177
CAS No:137219-37-5
Synonyms/Alias:aplidin;aplidine;plitidepsin;dehydrodidemnin B;
Plitidepsin is a cyclic depsipeptide originally isolated from the marine tunicate Aplidium albicans and is now produced synthetically for research purposes. As a complex peptide compound, it features a distinctive structure comprising both amino acid and hydroxy acid residues, which confers unique chemical and biological properties. Its molecular architecture enables specific interactions with various cellular proteins, making it a valuable tool for probing protein synthesis pathways, cell signaling mechanisms, and the regulation of intracellular processes. Researchers are particularly interested in plitidepsin due to its capacity to modulate eukaryotic elongation factor 1A (eEF1A), a critical component in translational control and cellular homeostasis. The compound's marine origin and well-defined peptide structure have positioned it as an important molecule in the study of peptide-based bioactivity and structure-function relationships.
Mechanistic studies: Plitidepsin is widely utilized in mechanistic investigations focused on the modulation of eEF1A, a pivotal protein involved in the elongation phase of mRNA translation. By enabling selective inhibition or modulation of eEF1A activity, the compound allows researchers to dissect the downstream effects on protein synthesis, cellular stress responses, and apoptotic pathways. These studies are instrumental in elucidating the molecular basis of translational regulation and the broader implications for cell growth and survival.
Peptide-protein interaction research: The unique depsipeptide structure of plitidepsin makes it an excellent probe for studying peptide-protein interactions, particularly those involving marine-derived natural products. Its ability to bind with high specificity to target proteins provides valuable insights into the conformational requirements and binding dynamics of cyclic peptides. Such research supports the rational design of novel peptide-based modulators and enhances understanding of how secondary structure influences biological activity.
Chemical biology tool development: As a structurally complex and biologically active peptide, plitidepsin serves as an important chemical biology tool for interrogating cellular pathways. It is frequently employed in high-content screening assays, target identification studies, and cellular phenotyping experiments. These applications facilitate the discovery of new molecular targets and help delineate the cellular networks responsive to peptide-based modulation, thereby advancing peptide chemistry and functional genomics.
Structure-activity relationship (SAR) studies: Plitidepsin is a key reference compound in SAR analyses aimed at understanding how specific modifications to peptide scaffolds influence biological function. By serving as a template for analog synthesis and comparative activity profiling, it enables researchers to map critical structural features responsible for target engagement and bioactivity. These studies inform the design of next-generation peptide compounds with improved selectivity, potency, or stability for research applications.
Analytical method development: The physicochemical complexity of plitidepsin has made it a valuable standard in the development and validation of analytical techniques for peptide and depsipeptide compounds. Its use in method optimization for high-performance liquid chromatography (HPLC), mass spectrometry, and related analytical platforms supports accurate quantification, purity assessment, and structural characterization of synthetic and natural peptides. This facilitates robust quality control and enhances the reliability of peptide research workflows.
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