Polymyxin B nonapeptide TFA contains a truncated peptide core that mirrors key structural features of the parent cyclic lipopeptide. Its cationic residues support analysis of membrane interactions and charge-dependent binding. The trifluoroacetate form improves solubility and experimental consistency. Research spans antimicrobial peptide modeling, lipid-peptide interactions, and sequence-activity correlation studies.
CAT No: R2201
CAS No:2220175-42-6
Synonyms/Alias:Polymyxin B nonapeptide TFA;2220175-42-6;(2S,3R)-2-Amino-N-((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)-3-hydroxybutanamide2,2,2;HY-106783A;DA-66797;CS-0128232;G17443;(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;2,2,2-trifluoroacetic acid;
Polymyxin B nonapeptide TFA is a synthetic peptide derivative obtained by enzymatic or chemical cleavage of the parent antibiotic polymyxin B, with the removal of its N-terminal fatty acyl group. As a cationic cyclic nonapeptide, it retains the characteristic amphipathic structure of polymyxins but lacks direct bactericidal activity. Its unique biochemical properties make it a valuable tool in membrane biology, antibiotic mechanism studies, and research into bacterial resistance pathways. Polymyxin B nonapeptide TFA is widely used in laboratories investigating the interactions between antimicrobial peptides and cell membranes, as well as in the development of novel agents targeting Gram-negative pathogens.
Membrane permeability studies: One of the principal applications of polymyxin B nonapeptide TFA is in the investigation of bacterial outer membrane permeability. Due to its preserved cyclic peptide core, it is capable of binding to lipopolysaccharide (LPS) components of Gram-negative bacterial membranes without causing cell lysis. This property allows researchers to dissect the specific interactions between cationic peptides and membrane phospholipids, providing mechanistic insight into the role of the fatty acyl tail in membrane disruption and the overall process of antimicrobial peptide-induced permeabilization.
Antibiotic mechanism elucidation: The nonapeptide serves as a critical negative control in studies aimed at understanding the mode of action of polymyxins. By comparing the biological activity of the nonapeptide fragment with that of the full-length antibiotic, researchers can differentiate the contributions of the peptide backbone and the fatty acyl moiety to antimicrobial efficacy. This comparative approach is essential for dissecting the molecular determinants of polymyxin-mediated bactericidal activity and for guiding the rational design of next-generation lipopeptide antibiotics.
Endotoxin neutralization assays: Polymyxin B nonapeptide TFA is frequently utilized in assays designed to study the neutralization of endotoxins, particularly lipopolysaccharides. Although it does not exhibit potent antimicrobial activity, its strong affinity for LPS enables its use as a probe to map and quantify LPS-peptide interactions. This application is important for the evaluation of potential endotoxin-neutralizing agents and for elucidating the structural requirements for effective LPS binding without concomitant cytotoxicity.
Peptide structure-function analysis: The nonapeptide fragment is a valuable model for structure-activity relationship (SAR) studies within the field of antimicrobial peptides. By employing it in biophysical and biochemical assays, scientists can probe the influence of peptide cyclization, charge distribution, and sequence modifications on membrane association, LPS binding, and aggregation behavior. These analyses contribute to a deeper understanding of the molecular features governing peptide function and inform the engineering of synthetic analogs with tailored biological properties.
Analytical method development: In addition to its functional studies, polymyxin B nonapeptide TFA is often used as a reference standard or analytical probe in chromatographic and mass spectrometric methods. Its well-defined structure and distinct physicochemical characteristics facilitate the calibration of analytical instruments and the validation of peptide detection protocols. This application supports quality control in peptide synthesis, purity assessment, and the development of robust methodologies for peptide quantification in complex biological matrices.
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