Polymyxin B nonapeptide is a cyclic peptide obtained from Polymyxin B by proteolytic removal of its terminal amino acyl residue. Polymyxin B nonapeptide is less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing th
CAT No: R1623
CAS No:86408-36-8
Synonyms/Alias:PMBN;86408-36-8;(2S,3R)-2-amino-N-[(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]-3-hydroxybutanamide;CHEMBL501248;SCHEMBL21498184;PYHYGIPVYYRJHU-QWDNBKTCSA-N;HY-106783;CS-0026547;G12497;
Polymyxin B nonapeptide is a cyclic peptide derivative obtained by enzymatic or chemical removal of the terminal fatty acyl tail from the parent antibiotic polymyxin B. As a structurally defined lipopeptide fragment, it retains the core cyclic nonapeptide ring while lacking the hydrophobic tail responsible for membrane-disruptive activity. This unique composition imparts distinctive biochemical properties, making Polymyxin B nonapeptide a highly valuable tool in membrane biology, endotoxin research, and peptide structure-function studies. Its ability to interact with bacterial outer membrane components, particularly lipopolysaccharides (LPS), without exerting significant cytotoxicity, has established it as an important reagent for dissecting the mechanistic basis of peptide-membrane interactions and for selectively probing endotoxin-related pathways in vitro.
Membrane interaction studies: Polymyxin B nonapeptide serves as a critical probe in the analysis of peptide-lipid interactions, especially for elucidating the role of the cyclic peptide domain in binding to Gram-negative bacterial membranes. Researchers utilize it to differentiate the contributions of the peptide core from those of the fatty acyl tail in membrane permeabilization, aggregation, and translocation phenomena. Its defined structure allows for precise biophysical assays, such as surface plasmon resonance, isothermal titration calorimetry, and fluorescence spectroscopy, to map binding affinities and conformational changes upon interaction with lipid bilayers or purified LPS.
Endotoxin neutralization assays: The compound is widely adopted in the assessment of LPS-binding affinity and specificity, providing a benchmark for evaluating the structure-activity relationships of polymyxin derivatives. Its selective affinity for the lipid A moiety of LPS, without the potent membrane-disruptive action of the parent compound, enables researchers to study endotoxin neutralization mechanisms in a controlled manner. This is particularly valuable for developing and validating new LPS detection or removal strategies in pharmaceutical and bioprocessing contexts, where minimizing cytotoxicity is essential.
Peptide structure-function research: Polymyxin B nonapeptide is instrumental in dissecting the structural determinants of antimicrobial peptide activity. By comparing its biochemical and biophysical properties to those of full-length polymyxin B and other analogs, scientists can delineate the roles of cyclic peptide conformation, charge distribution, and specific amino acid residues in mediating target recognition and biological activity. Such studies inform the rational design of novel peptide mimetics with tailored functionalities for research and industrial applications.
Analytical method development: The defined molecular structure and characteristic interactions of this nonapeptide make it a useful reference standard in chromatographic and mass spectrometric analyses. It is employed as a calibrant or internal standard for the qualitative and quantitative determination of polymyxin-related peptides in complex biological or pharmaceutical samples. Its use in method development supports accurate detection, identification, and quantification of lipopeptide derivatives in quality control and research workflows.
Cell culture and endotoxin removal evaluation: In the context of bioprocessing and cell-based assays, Polymyxin B nonapeptide is utilized to assess the efficacy and specificity of endotoxin removal procedures. Its ability to bind LPS without significant cytotoxicity makes it suitable for testing and optimizing resin or membrane-based endotoxin clearance systems. Researchers rely on it to validate the performance of purification protocols intended to reduce LPS contamination in recombinant protein production, ensuring the reliability of downstream cell culture experiments and analytical assays.
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
3. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
4. Myotropic activity of allatostatins in tenebrionid beetles
5. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More