Polymyxin B2 presents a lipopeptide structure rich in cationic and hydrophobic regions, facilitating membrane-interaction research. Cyclic and linear domains contribute to its complex conformational behavior. Researchers study charge-driven binding and lipid association. Applications include antimicrobial-peptide modeling, structural biophysics, and sequence-activity analysis.
CAT No: R2696
CAS No:34503-87-2
Synonyms/Alias:34503-87-2;UNII-99SJO09VH2;99SJO09VH2;CHEBI:59063;4,10-anhydro[N-(6-methylheptanoyl)-L-2,4-diaminobutanoyl-L-threonyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-D-phenylalanyl-L-leucyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-L-threonine];L-Threonine, N2-(6-methyl-1-oxoheptyl)-L-2,4-diaminobutanoyl-L-threonyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-D-phenylalanyl-L-leucyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-, cyclic (10-4)-peptide;N-[(2S)-4-amino-1-[[(2S,3R)-1-[[(2S)-4-amino-1-oxo-1-[[(3S,6S,9S,12S,15R,18S,21S)-6,9,18-tris(2-aminoethyl)-15-benzyl-3-[(1R)-1-hydroxyethyl]-12-(2-methylpropyl)-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptazacyclotricos-21-yl]amino]butan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-1-oxobutan-2-yl]-6-methylheptanamide;N-((S)-4-amino-1-(((2S,3R)-1-(((S)-4-amino-1-oxo-1-(((3S,6S,9S,12S,15R,18S,21S)-6,9,18-tris(2-aminoethyl)-15-benzyl-3-((R)-1-hydroxyethyl)-12-isobutyl-2,5,8,11,14,17,20-heptaoxo-1,4,7,10,13,16,19-heptaazacyclotricosan-21-yl)amino)butan-2-yl)amino)-3-hydroxy-1-oxobutan-2-yl)amino)-1-oxobutan-2-yl)-6-methylheptanamide;N2-(6-METHYL-1-OXOHEPTYL)-L-2,4-DIAMINOBUTANOYL-L-THREONYL-L-2,4-DIAMINOBUTANOYL-L-2,4-DIAMINOBUTANOYL-L-2,4-DIAMINOBUTANOYL-D-PHENYLALANYL-L-LEUCYL-L-2,4-DIAMINOBUTANOYL-L-2,4-DIAMINOBUTANOYL-L-THREONINE (10->4)-LACTAM;DTXSID20858929;Polysporin (TN);4,10-anhydro(N-(6-methylheptanoyl)-L-2,4-diaminobutanoyl-L-threonyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-D-phenylalanyl-L-leucyl-L-2,4-diaminobutanoyl-L-2,4-diaminobutanoyl-L-threonine);Polymyxin B sulphate?;SCHEMBL534885;CHEMBL1088938;HY-A0248B;DTXCID40809615;CS-0019930;D08401;Q27126427;
Polymyxin B2 is a potent cationic lipopeptide antibiotic derived from the bacterium Bacillus polymyxa, renowned for its unique structure and strong affinity for the outer membranes of Gram-negative bacteria. As a member of the polymyxin family, Polymyxin B2 is distinguished by its cyclic peptide backbone and fatty acid tail, which together confer remarkable membrane-disruptive capabilities. Its amphipathic nature enables it to interact intimately with lipid A components of lipopolysaccharides, making it a valuable tool in both microbiological research and biochemical applications. Due to its distinct mode of action, Polymyxin B2 has become an essential compound for scientists seeking to investigate bacterial membrane dynamics, resistance mechanisms, and the molecular basis of antimicrobial activity.
Antibacterial Research: In antibacterial research, Polymyxin B2 serves as a reference compound for evaluating the permeability and integrity of Gram-negative bacterial membranes. Researchers utilize it to selectively disrupt outer membrane structures, allowing for the assessment of bacterial susceptibility and resistance mechanisms. By exposing bacterial cultures to this lipopeptide, scientists can monitor changes in membrane potential, efflux pump activity, and the upregulation of protective genes, thereby deepening the understanding of how bacteria respond to membrane-targeting agents. Its ability to permeabilize the outer membrane also facilitates the delivery of other experimental agents, making it an invaluable tool for combinatorial studies.
Membrane Biology Studies: The unique interaction of Polymyxin B2 with lipid bilayers renders it highly useful in membrane biology studies. Investigators employ it to probe the biophysical properties of bacterial membranes, such as fluidity, lipid phase behavior, and the organization of membrane microdomains. By incorporating fluorescent probes or utilizing advanced imaging techniques, researchers can visualize the real-time effects of this peptide on membrane architecture. These studies provide critical insights into the role of specific lipid components in maintaining membrane integrity and the mechanisms underlying membrane disruption by cationic peptides.
Endotoxin Neutralization: Polymyxin B2 is widely applied in the neutralization of endotoxins, particularly lipopolysaccharides (LPS) from Gram-negative bacteria, in various research settings. Its strong binding affinity for lipid A allows it to sequester and inactivate LPS, minimizing the confounding effects of endotoxin contamination in cell culture experiments and protein preparations. This property is especially valuable in immunological assays, where even trace amounts of LPS can trigger nonspecific inflammatory responses. By incorporating the peptide into experimental workflows, researchers can ensure more accurate interpretation of immune signaling and cytokine production data.
Analytical Method Development: In the field of analytical chemistry, Polymyxin B2 is employed in the development and validation of assays designed to detect and quantify endotoxins or to monitor the presence of Gram-negative bacterial contaminants. Its specificity for LPS enables the creation of sensitive detection platforms, such as biosensors or chromatographic methods, that rely on its selective binding properties. These analytical tools are critical for quality control in biopharmaceutical manufacturing, environmental monitoring, and food safety testing, where rapid and reliable detection of endotoxins or bacterial contaminants is paramount.
Antimicrobial Resistance Mechanism Studies: The role of Polymyxin B2 in elucidating antimicrobial resistance mechanisms has garnered significant attention in recent years. By subjecting bacterial strains to controlled exposures of this compound, researchers can induce and characterize resistance phenotypes, analyze genetic mutations, and study adaptive responses at the molecular level. These investigations are crucial for identifying novel resistance genes, understanding the evolution of multidrug-resistant pathogens, and informing the design of next-generation membrane-targeting agents. The peptide's well-characterized mode of action and established research protocols make it a cornerstone in the ongoing battle against antimicrobial resistance.
Biophysical Characterization of Peptide-Lipid Interactions: Scientists frequently employ Polymyxin B2 in the biophysical characterization of peptide-lipid interactions, utilizing techniques such as isothermal titration calorimetry, surface plasmon resonance, and nuclear magnetic resonance spectroscopy. These studies elucidate the thermodynamics, kinetics, and structural determinants of its binding to various lipid species, advancing the broader understanding of peptide-membrane interactions. Insights gained from such research inform the rational design of novel antimicrobial peptides and contribute to the development of innovative strategies for targeting bacterial membranes, reinforcing Polymyxin B2's status as an indispensable tool in both fundamental and applied bioscience research.
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