Murepavadin (POL7080) is a highly potent, specific, macrocycle Pseudomonas antibiotic for the treatment of bacterial infections caused by Pseudomonas aeruginosa.
CAT No: R1900
CAS No:944252-63-5
Synonyms/Alias:Murepavadin;944252-63-5;Murepavadin [INN];POL7080;RO7033877;Murepavadina;Murepavadine;0D02GRY87Z;Murepavadin [USAN:INN];UNII-0D02GRY87Z;RO-7033877;POL-7080;MUREPAVADIN [USAN];MUREPAVADIN [WHO-DD];Cyclo(L-alanyl-L-seryl-D-prolyl-L-prolyl-L-threonyl-L-tryptophyl-L-isoleucyl-(2S)-2,4-diaminobutanoyl-L-ornithyl-(2R)-2,4-diaminobutanoyl-(2S)-2,4-diaminobutanoyl-L-tryptophyl-(2S)-2,4-diaminobutanoyl-(2S)-2,4-diaminobutanoyl);RG7929;RG-7929;MUREPAVADIN TFA;murepavadinum;Murepavadin TFA salt;Murepavadin (USAN/INN);Murepavadin (POL7080);POL7080 TFA;CHEMBL3946483;GTPL10832;EX-A4063;UMB25263;AKOS037648482;DB14777;BS-14122;DA-65706;D10957;D80443;Q27236621;cyclo(-L-threonyl-L-tryptophanyl-L-isoleucyl-L-2,4-diaminobutyryl-L-ornithyl-D-2,4-diaminobutyryl-L-2,4-diaminobutyryl-L-tryptophanyl-L-2,4-diaminobutyryl-L-2,4-diaminobutyryl-L-alanyl-L-seryl-D-prolyl-L-prolyl), acetate salt;
Chemical Name:(3R,9S,12S,15S,18S,21S,24S,27R,30S,33S,36S,39S,42S,45S)-15,18,24,27,33-pentakis(2-aminoethyl)-30-(3-aminopropyl)-36-[(2S)-butan-2-yl]-42-[(1R)-1-hydroxyethyl]-9-(hydroxymethyl)-21,39-bis(1H-indol-3-ylmethyl)-12-methyl-1,7,10,13,16,19,22,25,28,31,34,37,40,43-tetradecazatricyclo[43.3.0.03,7]octatetracontane-2,8,11,14,17,20,23,26,29,32,35,38,41,44-tetradecone
Murepavadin is a synthetic cyclic peptide antibiotic that specifically targets Gram-negative bacteria, most notably Pseudomonas aeruginosa, by binding to the outer membrane protein LptD and disrupting lipopolysaccharide transport. As a member of the peptidomimetic class, it is structurally engineered to mimic natural host-defense peptides, conferring both stability and highly selective antimicrobial activity. Its unique mechanism of action and specificity for Pseudomonas species have made it a subject of significant interest in microbiology, antimicrobial resistance research, and peptide structure-function studies. Murepavadin's biochemical properties and targeted bacterial interaction profile support its use in a variety of advanced research applications focused on bacterial membrane biology, peptide antibiotic design, and the study of resistance mechanisms.
Antimicrobial mechanism studies: Researchers employ murepavadin to elucidate the molecular basis of outer membrane disruption in Gram-negative bacteria, particularly through its high-affinity interaction with LptD. By using this peptide in controlled assays, investigators can dissect the sequence of events leading to membrane destabilization, explore the downstream effects on bacterial viability, and compare its mode of action to other peptide-based antibiotics. Such studies provide valuable insights into the structure-activity relationships that underpin selective bacterial targeting and inform the rational design of next-generation antimicrobial agents.
Resistance mechanism investigations: The compound serves as a powerful tool for studying the development of resistance in Pseudomonas aeruginosa and related species. By exposing bacterial cultures to murepavadin under various conditions, researchers can monitor genetic and phenotypic adaptations that confer reduced susceptibility. These experiments enable the identification of resistance pathways, such as mutations in LptD or alterations in membrane composition, and facilitate the evaluation of strategies to overcome or prevent resistance. The findings contribute to a deeper understanding of how bacteria respond to selective pressure from peptide antibiotics.
Peptide structure-function analysis: Murepavadin is frequently utilized as a model system in peptide chemistry and structural biology to investigate the relationship between peptide conformation, target binding, and antimicrobial efficacy. Through the application of techniques such as NMR spectroscopy, X-ray crystallography, and molecular dynamics simulations, scientists can characterize its three-dimensional structure and dynamic interactions with bacterial membrane proteins. These analyses not only elucidate the determinants of specificity and potency but also guide the optimization of peptide scaffolds for improved activity and stability.
Antibacterial screening and assay development: The compound is incorporated into high-throughput screening platforms and susceptibility assays designed to evaluate the efficacy of novel antimicrobial candidates or to benchmark the activity of other peptide antibiotics. Its well-characterized mechanism and selective action make it an ideal positive control or reference compound in in vitro studies assessing bacterial viability, membrane integrity, or synergistic effects with other agents. Such applications support the discovery and validation of new antibacterial compounds and the refinement of assay methodologies.
Membrane protein interaction research: Murepavadin's selective binding to LptD has established it as a valuable probe for exploring the structure, function, and inhibition of bacterial outer membrane protein complexes. By leveraging its specificity, investigators can dissect the role of LptD in lipopolysaccharide transport, study the molecular determinants of protein-peptide recognition, and develop assays to screen for additional inhibitors targeting this essential pathway. These research directions advance the broader understanding of bacterial envelope biogenesis and the potential for targeting membrane proteins in antimicrobial development.
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