Polymyxin B1 is a cationic lipopeptide that exhibits strong affinity for lipid bilayers through hydrophobic-electrostatic complementarity. Its cyclic and linear domains generate a rigid yet amphipathic scaffold. Researchers study its membrane-disruption mechanisms and binding thermodynamics. Applications include antimicrobial-peptide modeling, lipid-interaction studies, and sequence-activity profiling.
CAT No: R2569
CAS No:4135-11-9
Synonyms/Alias:4135-11-9;UNII-B35S89JSRU;B35S89JSRU;(6S)-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-methyloctanamide;CHEMBL2397513;BRN 0505906;L-THREONINE, N2-(6-METHYL-1-OXOOCTYL)-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;N2-(6-METHYL-1-OXOOCTYL)-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 CYCLIC (10->4)-PEPTIDE;CHEBI:8309;DTXSID80858844;DTXCID1028441;SCHEMBL14241069;HY-A0248A;BDBM50548037;MS-32043;CS-0019929;(S)-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;
Polymyxin B1 is a prominent member of the polymyxin antibiotic family, recognized for its unique cyclic peptide structure and potent activity against Gram-negative bacteria. As a cationic lipopeptide, Polymyxin B1 demonstrates a strong affinity for the lipopolysaccharide (LPS) components of bacterial outer membranes, facilitating its role as both a research tool and a reference compound in microbiological studies. Its amphipathic nature enables it to disrupt membrane integrity, making it an invaluable resource in investigations related to bacterial physiology, resistance mechanisms, and membrane-targeted therapeutics. The compound's stability and well-characterized mechanism of action have positioned it as a standard in evaluating the efficacy and mode of action of novel antimicrobial agents, as well as in exploring the fundamental properties of bacterial membranes.
Antibiotic Mechanism Studies: Polymyxin B1 is extensively utilized in elucidating the mechanisms of bacterial membrane disruption. By interacting with the lipid A component of bacterial LPS, it destabilizes the outer membrane, leading to increased permeability and cell death. Researchers employ Polymyxin B1 to dissect the sequence of molecular events following membrane targeting, enabling a deeper understanding of how peptides compromise bacterial defenses. These insights are crucial for the development of next-generation antimicrobials that can circumvent existing resistance pathways.
Antimicrobial Susceptibility Testing: In microbiology laboratories, Polymyxin B1 serves as a benchmark compound for antimicrobial susceptibility assays. Its well-documented activity spectrum against Gram-negative organisms makes it a preferred choice for determining the resistance profiles of clinical and environmental bacterial isolates. By incorporating it into standardized testing platforms, scientists can accurately assess how bacterial populations respond to lipopeptide antibiotics, facilitating surveillance of emerging resistance trends and guiding the optimization of antimicrobial regimens.
Membrane Biophysics Research: The unique mode of action of Polymyxin B1 has inspired its use in studies focused on the physicochemical properties of biological membranes. Researchers utilize this compound to probe membrane fluidity, permeability, and structural integrity in model systems such as liposomes or bacterial spheroplasts. By observing the biophysical changes induced by Polymyxin B1, scientists can gain valuable insights into membrane dynamics, lipid-protein interactions, and the general principles governing membrane-active agents.
Endotoxin Neutralization: Beyond its antimicrobial properties, Polymyxin B1 is widely employed in the neutralization of endotoxins in research and bioprocessing contexts. Its high affinity for the lipid A moiety of LPS enables it to bind and sequester endotoxins from biological samples, cell cultures, and recombinant protein preparations. This application is particularly important in minimizing the confounding effects of endotoxin contamination during in vitro experiments, ensuring the reliability and reproducibility of sensitive biological assays.
Analytical Reference Standard: Polymyxin B1 frequently functions as a reference material in analytical chemistry and quality control procedures. Laboratories rely on its well-characterized profile to calibrate chromatographic systems, validate bioassays, and assess the potency of related compounds. Its consistent behavior and established analytical signatures make it indispensable for method development and routine quality assurance in pharmaceutical and research settings. Collectively, these diverse application areas highlight the scientific value and versatility of Polymyxin B1, underscoring its enduring relevance in microbiology, biochemistry, and pharmaceutical research.
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