Bactenecin is a cysteine-rich antimicrobial peptide forming stable disulfide-linked structures. Researchers employ it to explore β-sheet stabilization, membrane interaction, and redox behavior. The sequence supports examination of peptide folding in hydrophobic environments. Its unusual architecture allows detailed structural mapping.
CAT No: R2287
CAS No:116229-36-8
Synonyms/Alias:Bactenecin;116229-36-8;Arg-leu-cyclo(cys-arg-ile-val-val-ile-arg-val-cys)-arg;Bactenecin, bovine;Bac7;CHEBI:201834;2-[[28-[[2-[[2-amino-5-(diaminomethylideneamino)pentanoyl]amino]-4-methylpentanoyl]amino]-13,22-di(butan-2-yl)-10,25-bis[3-(diaminomethylideneamino)propyl]-6,9,12,15,18,21,24,27-octaoxo-7,16,19-tri(propan-2-yl)-1,2-dithia-5,8,11,14,17,20,23,26-octazacyclononacosane-4-carbonyl]amino]-5-(diaminomethylideneamino)pentanoic acid;DA-61475;PD150815;
Bactenecin is a cationic antimicrobial peptide originally isolated from bovine neutrophils, recognized for its broad-spectrum activity against Gram-negative and Gram-positive bacteria. As a member of the host defense peptide family, it features a distinctive cyclic structure stabilized by disulfide bonds, which contributes to its potent membrane-disrupting capabilities. Its relatively small size and robust antimicrobial properties have made it a valuable model in innate immunity research and peptide engineering. The unique biochemical features of bactenecin have positioned it as an important tool for exploring host-pathogen interactions, antimicrobial mechanisms, and the development of novel peptide-based applications in the life sciences.
Antimicrobial mechanism studies: Bactenecin is widely used in research aimed at elucidating the molecular basis of antimicrobial activity. Its well-characterized ability to interact with and disrupt microbial membranes provides a model system for investigating peptide-lipid interactions, pore formation, and the determinants of selective toxicity against bacterial versus eukaryotic cells. By serving as a reference peptide, it enables comparative studies that help define the physicochemical parameters underlying effective antimicrobial action.
Innate immunity research: As a naturally occurring component of the mammalian immune system, bactenecin is frequently utilized to study the role of antimicrobial peptides in innate defense mechanisms. Researchers employ it to examine how neutrophil-derived peptides contribute to pathogen clearance, modulate immune responses, and interact with other components of the immune network. Its use in in vitro and ex vivo assays supports the dissection of signaling pathways and immune modulation events linked to peptide-mediated host defense.
Peptide engineering and design: The structural and functional attributes of bactenecin make it a valuable template for the design of novel synthetic peptides with enhanced stability, specificity, or activity. Its sequence and disulfide-stabilized loop provide insights into the relationship between peptide conformation and biological function. Scientists leverage bactenecin as a scaffold for rational design, site-directed mutagenesis, and the creation of peptide analogs intended for improved antimicrobial properties or tailored bioactivity profiles.
Microbial resistance studies: The use of bactenecin in laboratory models allows researchers to investigate mechanisms of bacterial resistance to cationic peptides. By exposing microbial populations to repeated peptide challenge, scientists can monitor adaptive responses, identify genetic determinants of resistance, and evaluate the efficacy of combination strategies to mitigate resistance development. These studies contribute to a deeper understanding of microbial adaptation and inform the design of next-generation antimicrobial agents.
Analytical and assay development: Bactenecin serves as a benchmark compound in the development and validation of antimicrobial susceptibility assays, membrane interaction studies, and peptide quantification methods. Its defined activity profile and structural characteristics make it suitable for calibrating bioassays, optimizing chromatographic separations, and establishing quality control protocols in peptide research laboratories. By providing a consistent standard, it supports reproducibility and comparability across experimental platforms.
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