Elisidepsin, an innovative biomedicine with remarkable capabilities, emerges as a formidable weapon in the battle against cancer. Employed in the treatment of diverse tumor types such as breast and prostate cancer, this powerful compound unveils its true potential in thwarting tumor progression. By selectively targeting and perturbing cellular membranes, Elisidepsin effectively hamstrings relentless tumor growth, pledging to unleash a cascade of cancer cell demise. The unparalleled prowess exhibited by this product instills hope within the medical community, offering a novel therapeutic avenue for those afflicted with advanced cancer.
CAT No: R2035
CAS No:681272-30-0
Chemical Name:(2R)-N-[(2S)-5-amino-1-[[(2R,3S)-1-[[(3S,6Z,9S,12R,15R,18R,19R)-9-benzyl-15-[(2S)-butan-2-yl]-6-ethylidene-19-methyl-2,5,8,11,14,17-hexaoxo-3,12-di(propan-2-yl)-1-oxa-4,7,10,13,16-pentazacyclononadec-18-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]-1-[(2R)-2-[[(2S)-2-[[(2S,3R)-3-hydroxy-2-[[(2R)-3-methyl-2-[[(4S)-4-methylhexanoyl]amino]butanoyl]amino]butanoyl]amino]-3-methylbutanoyl]amino]-3-methylbutanoyl]pyrrolidine-2-carboxamide
Elisidepsin is a synthetic cyclic peptide belonging to the class of depsipeptides, notable for its unique structural motifs and membrane-interacting properties. As a marine-derived compound originally inspired by natural products, Elisidepsin has garnered significant attention in biochemical and pharmacological research due to its ability to disrupt cellular membranes and modulate lipid bilayer integrity. Its distinctive amphipathic character and propensity for interacting with specific membrane components make it a valuable molecular tool for investigating mechanisms of membrane dynamics, peptide-membrane interactions, and the functional consequences of lipid perturbation. Elisidepsin's relevance extends across peptide chemistry, cellular biochemistry, and the study of bioactive marine compounds, positioning it as a critical reagent for advanced research applications.
Membrane interaction studies: Elisidepsin is widely utilized in research focused on elucidating the mechanisms of peptide-lipid interactions and membrane disruption. Its ability to integrate into and destabilize phospholipid bilayers provides a robust model for examining the biophysical principles underlying membrane-active peptides. Researchers employ it to probe the specificity and dynamics of peptide-induced membrane permeabilization, supporting the development of new paradigms in membrane biochemistry and the design of next-generation amphipathic peptides.
Peptide structure-activity relationship analysis: The structurally unique features of this cyclic depsipeptide make it an exemplary subject for structure-activity relationship (SAR) investigations. By systematically modifying its amino acid sequence or depsipeptide linkages, scientists can assess how specific structural elements influence biological activity, membrane affinity, and selectivity. Such studies are instrumental in guiding the rational design of synthetic peptides with tailored physicochemical properties for research and industrial purposes.
Cell signaling and apoptosis research: Elisidepsin's capacity to induce membrane destabilization has been harnessed to study downstream effects on cellular signaling pathways, particularly those involved in programmed cell death. In vitro systems benefit from its use as a tool to trigger or modulate apoptosis via membrane perturbation, enabling detailed dissection of the molecular events that link membrane integrity to intracellular signaling cascades. This application is especially relevant for elucidating the interplay between membrane-active compounds and cell fate decisions.
Marine natural product analog research: As a synthetic analog inspired by marine-derived peptides, Elisidepsin serves as a reference compound in the exploration of marine natural product chemistry. Its use enables comparative studies aimed at understanding the structure and function of marine depsipeptides, supporting efforts to identify new bioactive molecules from marine organisms. Such comparative analyses facilitate the discovery and optimization of novel peptide scaffolds with desirable research properties.
Analytical method development: The distinct chemical characteristics of this peptide make it a valuable standard in the development and validation of analytical techniques, including high-performance liquid chromatography (HPLC) and mass spectrometry. Its defined structure and membrane-active profile enable method optimization for the detection, quantification, and characterization of cyclic peptides and related compounds in complex biological matrices. By serving as a model analyte, it supports the advancement of analytical protocols essential for peptide research and quality assessment.
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