Amphomycin exhibits broad-spectrum activity against Gram-positive bacteria and is particularly effective against drug-resistant strains. Amphomycin is commonly used as a therapeutic option for treating infections caused by Methicillin-resistant Staphylococcus aureus (MRSA) and Enterococcus species.
CAT No: R2053
CAS No:1402-82-0
Chemical Name:(3S)-4-[[(3S,4R,7S,13S,16R,22S,28S,31S,34R)-16-(1-aminoethyl)-31-[(1S)-1-carboxyethyl]-22,28-bis(carboxymethyl)-4-methyl-2,6,12,15,18,21,24,27,30,33-decaoxo-13-propan-2-yl-1,5,11,14,17,20,23,26,29,32-decazatricyclo[32.4.0.07,11]octatriacontan-3-yl]amino]-3-[[(Z)-10-methyldodec-3-enoyl]amino]-4-oxobutanoic acid
Amphomycin is a cyclic lipopeptide antibiotic produced by certain Streptomyces species, recognized for its unique structure and its ability to interact with bacterial cell wall biosynthesis. As a member of the peptide compound family, Amphomycin possesses a distinct cyclic peptide core linked to a fatty acid side chain, which underpins its biological activity. Its mechanism of action primarily involves the inhibition of cell wall formation in Gram-positive bacteria through interference with peptidoglycan synthesis, making it a valuable tool for scientific exploration of bacterial physiology and cell wall-targeted processes. The compound's structural and functional characteristics have positioned it as an important research molecule in microbiology, biochemistry, and antimicrobial drug discovery.
Antibiotic mechanism research: Amphomycin is widely utilized in studies investigating the molecular mechanisms underlying lipopeptide antibiotics. Researchers employ it to dissect the specific interactions between cyclic lipopeptides and bacterial membrane components, particularly the binding to undecaprenyl pyrophosphate, a lipid carrier essential in peptidoglycan biosynthesis. By elucidating these interactions, scientists gain deeper insight into the mode of action of peptide antibiotics and the molecular basis for their selective toxicity towards bacterial cells, thereby advancing the understanding of antimicrobial resistance and informing the rational design of new antibacterial agents.
Cell wall biosynthesis studies: The compound serves as a critical probe in experimental systems designed to examine bacterial cell wall assembly and regulation. Its ability to inhibit the translocation of peptidoglycan precursors provides a precise means to arrest and analyze stages of cell wall formation. This enables researchers to delineate the roles of specific enzymes, transporters, and intermediates in peptidoglycan metabolism, contributing to the mapping of cell wall biosynthetic pathways and the identification of potential vulnerabilities in pathogenic bacteria.
Antimicrobial screening and assay development: Amphomycin is frequently employed as a reference compound or positive control in antimicrobial susceptibility testing, high-throughput screening assays, and validation of novel antibiotic candidates. Its well-characterized activity profile against Gram-positive organisms makes it an ideal benchmark for evaluating the efficacy and specificity of new compounds targeting cell wall synthesis. These applications support the development of robust, reproducible assay platforms critical for antibiotic discovery and resistance monitoring in both academic and industrial research settings.
Structure-activity relationship (SAR) investigations: The unique cyclic lipopeptide structure of Amphomycin provides a valuable template for SAR studies aimed at optimizing peptide-based antibiotics. Chemical modification and analog synthesis experiments use it as a starting point to probe the impact of structural variations on biological activity, membrane interaction, and target specificity. Insights gained from these SAR studies inform the development of next-generation lipopeptide therapeutics and enhance the fundamental understanding of peptide-membrane interactions and antibiotic design principles.
Microbial bioproduction and biosynthetic pathway research: The biosynthesis of Amphomycin by Streptomyces species offers a model system for exploring nonribosomal peptide synthetase (NRPS) pathways and natural product engineering. Researchers utilize it to investigate the genetic and enzymatic machinery responsible for complex lipopeptide assembly, with the goal of elucidating biosynthetic logic and enabling the biotechnological production of novel peptide antibiotics. These studies facilitate advances in synthetic biology, metabolic engineering, and the discovery of new bioactive natural products with potential research and industrial applications.
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