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| CAS:302327-42-0:Friulimicin D | |
| Friulimicin D is a novel cyclic lipopeptide antibiotic produced by Actinoplanes friuliensis fermentation. It exerts bactericidal effect by binding bacterial cell wall precursor Lipid II with high affinity and blocking peptidoglycan synthesis. It exhibits potent activity against multidrug-resistant Gram-positive bacteria such as MRSA and VRE. Applied in drug-resistant infection, novel antibiotic development and cell wall synthesis mechanism research. | |
| 90%/95%/98% | |
| Non-ribosomal acidic cyclic lipopeptide with fatty acid side chain modification | |
| ~1520 |
| Function Tags (comma-separated) | ||||||||
| Friulimicin D; Cyclic lipopeptide antibiotic; CAS 302327-42-0 | Anti-multidrug-resistant bacteria,Lipid II targeting,Cell wall synthesis inhibition,MRSA/VRE activity,Cyclic lipopeptide class,Novel antibiotic | Decapeptide backbone cyclized via head-to-tail amide bond, N-terminal branched fatty acid modification, multiple unnatural amino acids | Large cyclic lipopeptide, no precise small-molecule formula; subject to actual batch MS | - | ~1520 (theoretical) | Head-to-tail amide bond macrocyclization | Non-ribosomal acidic cyclic lipopeptide |
| Long-term Storage Conditions | Short-term Storage Conditions | ||||
| PEP-FRD001 | Store at -20℃, sealed, dry & protected from light, aliquoted; avoid high temperature, humidity and strong acid/base | Solid powder stable for 2 years at 2-8℃ sealed and dry; stock solutions prepared in DMSO or methanol | Stable for 72 h at 4℃ under anhydrous conditions. Prone to aggregation in aqueous phase; **aqueous solutions must be prepared freshly before use**. **Extremely poor water solubility, DMSO required for solubilization**. Fatty acid side chain tends to cause aqueous phase self-aggregation. Unsaturated bonds prone to oxidative degradation under light | Stable for 2 years at -20℃ under dry & dark conditions |
| Applicable Research Areas (comma-separated) | ||||
| PEP-FRD001 | Novel acidic cyclic lipopeptide antibiotic that targets Lipid II to block cell wall synthesis, potent against multidrug-resistant Gram-positive bacteria | Friulimicin D is a member of the natural cyclic lipopeptide antibiotic family, produced by Actinomycetes via the non-ribosomal peptide synthesis pathway, with a unique acidic cyclic peptide backbone and branched fatty acid side chain. Its mechanism differs from the membrane disruption effect of daptomycin: it binds with high affinity to the cell wall precursor Lipid II on the outer side of the bacterial cytoplasmic membrane, forms a stable complex and sterically blocks substrate binding of transglycosylase and transpeptidase, inhibits peptidoglycan chain elongation and cross-linking, disrupts cell wall biosynthesis, and ultimately leads to bacterial osmotic lysis. This molecule exhibits potent bactericidal activity against Gram-positive bacteria such as Staphylococcus aureus, Streptococcus and Enterococcus, and is also effective against clinical multidrug-resistant strains such as MRSA and VRE, with no cross-resistance to existing antibiotics. It serves as a core tool molecule for drug-resistant infection mechanism research, novel cell wall-targeted antibiotic development, and Lipid II binding peptide SAR analysis. | Drug-resistant infection research,Novel antibiotic development,Bacterial cell wall biology,Lipid II target study,MRSA/VRE research,Microbial pharmacology |
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