Polymyxin B3

Polymyxin B3 represents a lipopeptide-derived structure rich in cationic residues that support membrane-interaction studies. Its cyclic and linear elements create a multifaceted conformational profile. Researchers examine its binding behavior toward lipid assemblies. Applications include antimicrobial-peptide modeling, structural mimicry, and charge-driven interaction research.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Polymyxin B3(CAS 71140-58-4)

CAT No: R2468

CAS No:71140-58-4

Synonyms/Alias:DPMB3;UNII-L194HGU2LD;L194HGU2LD;71140-58-4;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]octanamide;CHEMBL1088939;SCHEMBL21474115;

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M.F/Formula
C55H96N16O13
M.W/Mr.
1189.5
Sequence
Three Letter Code:octanoyl-Dab-Thr-Dab-Dab(1)-Dab-D-Phe-Leu-Dab-Dab-Thr-(1)

Polymyxin B3 is a cyclic lipopeptide antibiotic that belongs to the polymyxin family, recognized for its potent activity against Gram-negative bacteria. As a naturally occurring peptide compound, Polymyxin B3 is distinguished by its amphipathic structure and strong affinity for bacterial membranes, making it a valuable tool in biochemical and microbiological research. Its unique mechanism of disrupting the outer membrane of susceptible bacteria has positioned it as a critical reference molecule for studying membrane-targeting agents, resistance mechanisms, and the molecular basis of antimicrobial activity. The compound's defined structure and well-characterized mode of action have made it a benchmark in the investigation of peptide-membrane interactions and in the development of novel antimicrobial strategies.

Antimicrobial Mechanism Studies: In the field of microbiology, Polymyxin B3 is widely utilized to elucidate the molecular interactions between lipopeptide antibiotics and bacterial outer membranes. Researchers employ it to dissect how cationic peptides bind to lipopolysaccharides and destabilize the membrane integrity of Gram-negative organisms. This application provides critical insights into the structure-activity relationships governing peptide-based antimicrobials and informs the rational design of next-generation compounds with improved selectivity and potency.

Resistance Mechanism Research: The compound serves as an essential tool in investigating bacterial resistance to peptide antibiotics. By exposing various Gram-negative strains to Polymyxin B3, scientists can characterize genetic and biochemical adaptations—such as modifications to lipid A or efflux pump expression—that confer reduced susceptibility. These studies are fundamental for understanding the evolving landscape of antimicrobial resistance and for identifying molecular targets to counteract resistance mechanisms.

Membrane Biophysics and Lipid Interaction Analysis: Polymyxin B3 is frequently employed in biophysical assays to probe membrane dynamics and lipid interactions. Its ability to induce permeability changes and membrane disruption allows researchers to model and quantify peptide-lipid binding events, membrane fluidity alterations, and vesicle leakage. Such investigations contribute to a deeper understanding of membrane-active peptides, their selectivity, and the physicochemical determinants of their biological activity.

Analytical Reference Standard: In analytical chemistry and quality control laboratories, Polymyxin B3 is used as a reference standard for the identification, quantification, and characterization of polymyxin compounds. Its defined structure and consistent activity profile make it suitable for calibration in chromatographic and mass spectrometric assays, supporting the accurate analysis of related lipopeptide antibiotics and ensuring methodological reliability in compound screening and purity assessments.

Peptide Synthesis and Structure-Function Studies: The compound's well-resolved sequence and established synthetic accessibility render it an important model in peptide chemistry. Synthetic analog development and structure-activity relationship studies often use Polymyxin B3 as a template to explore modifications that influence antimicrobial efficacy, toxicity, and pharmacodynamic properties. These efforts underpin the advancement of novel peptide-based agents and facilitate the optimization of peptide therapeutics for research applications.

InChI
InChI=1S/C55H96N16O13/c1-6-7-8-9-13-16-43(74)62-35(17-23-56)50(79)71-45(33(5)73)55(84)67-38(20-26-59)47(76)66-40-22-28-61-54(83)44(32(4)72)70-51(80)39(21-27-60)64-46(75)36(18-24-57)65-52(81)41(29-31(2)3)68-53(82)42(30-34-14-11-10-12-15-34)69-48(77)37(19-25-58)63-49(40)78/h10-12,14-15,31-33,35-42,44-45,72-73H,6-9,13,16-30,56-60H2,1-5H3,(H,61,83)(H,62,74)(H,63,78)(H,64,75)(H,65,81)(H,66,76)(H,67,84)(H,68,82)(H,69,77)(H,70,80)(H,71,79)/t32-,33-,35+,36+,37+,38+,39+,40+,41+,42-,44+,45+/m1/s1
InChI Key
MUZYEKLWXWDOOD-RUDZPDEXSA-N

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