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 cyclic lipopeptide antibiotic that belongs to the polymyxin family, distinguished by its potent activity against Gram-negative bacteria. As a secondary component of the Polymyxin B complex, it is characterized by a unique structure that includes a fatty acid tail and a cationic peptide ring, enabling strong interactions with bacterial membranes. Its primary mechanism of action involves binding to the lipid A portion of lipopolysaccharides, which disrupts membrane integrity and leads to cell lysis. Due to its well-defined mode of action and specificity, Polymyxin B2 has become an essential tool in microbiological and biochemical research focused on bacterial physiology, membrane biology, and antimicrobial resistance mechanisms.
Antimicrobial susceptibility testing: Polymyxin B2 is widely utilized in laboratory investigations to assess the susceptibility of various Gram-negative bacterial strains to polymyxin-class antibiotics. By incorporating this compound into agar diffusion or broth microdilution assays, researchers can accurately determine minimum inhibitory concentrations and characterize resistance patterns. This application is particularly valuable for tracking the emergence and prevalence of polymyxin resistance in clinical and environmental isolates, thereby supporting surveillance studies and informing future therapeutic research.
Membrane permeability studies: Due to its well-characterized membrane-disrupting properties, Polymyxin B2 serves as a model lipopeptide for probing bacterial outer membrane integrity. Researchers employ it to induce controlled permeabilization, which facilitates the study of membrane protein function, transport processes, and the role of lipopolysaccharides in barrier formation. By analyzing changes in membrane potential, ion flux, or the uptake of fluorescent dyes following exposure, investigators can elucidate the molecular basis of bacterial defense mechanisms and membrane dynamics.
Mechanistic investigations of antibiotic resistance: The defined structure and activity of Polymyxin B2 make it an ideal probe for dissecting the molecular determinants of polymyxin resistance. Studies frequently use it to examine the impact of lipid A modifications, efflux pump expression, or regulatory gene mutations on bacterial survival. By comparing the effects of this compound on wild-type versus mutant strains, researchers gain valuable insights into adaptive resistance pathways and potential targets for novel antimicrobial strategies.
Lipid-protein interaction analysis: The amphipathic nature of Polymyxin B2 allows it to interact selectively with lipid components of biological membranes, making it a useful reagent for studying lipid-protein interactions in vitro. It is often applied in biochemical assays to investigate how membrane-active peptides modulate the structure and function of integral membrane proteins. Such studies contribute to a deeper understanding of membrane organization, signaling, and the biophysical properties underlying cellular responses to external stressors.
Analytical reference standard: In quality control and analytical chemistry settings, Polymyxin B2 is employed as a reference material for the identification, quantification, and purity assessment of polymyxin mixtures. Its well-characterized chemical profile enables precise calibration of chromatographic and spectrometric methods, ensuring reliable detection of polymyxin components in complex samples. This application is critical for the development and validation of analytical protocols used in research, manufacturing, and environmental monitoring of antibiotic residues.
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