Indolicidin is a potent antimicrobial peptide purified from the cytoplasmic granules of bovine neutrophils.
CAT No: R1445
CAS No:140896-21-5
Synonyms/Alias:Indolicidin;140896-21-5;Tridecapeptide amide;AKOS040763967;DA-64442;NH2-Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-CONH2;
Indolicidin is a naturally occurring antimicrobial peptide originally isolated from bovine neutrophils, distinguished by its rich content of tryptophan and proline residues. As a member of the cathelicidin family, it exhibits a unique cationic and amphipathic structure that enables broad-spectrum activity against various microorganisms. The peptide's notable ability to interact with and disrupt microbial membranes has made it a significant subject of interest in biochemical and microbiological research. Its short, linear sequence and distinctive mode of action set it apart from many other host defense peptides, providing valuable insights into innate immunity and peptide-membrane interactions.
Antimicrobial mechanism studies: Indolicidin is widely utilized in research focused on elucidating the molecular mechanisms underlying antimicrobial activity. Its ability to permeabilize and destabilize bacterial and fungal membranes, as well as its interactions with intracellular targets such as DNA, make it a model system for studying non-lytic and lytic antimicrobial pathways. Researchers employ the peptide to dissect how cationic peptides recognize, bind to, and disrupt microbial cell envelopes, advancing the understanding of innate immune defense strategies and informing the design of synthetic analogs with optimized properties.
Membrane biophysics research: The unique amphipathic character and sequence composition of indolicidin render it an ideal tool for investigating peptide-lipid interactions in biophysical studies. By incorporating the peptide into model membrane systems such as liposomes, supported bilayers, or giant unilamellar vesicles, scientists can probe the structural and dynamic consequences of peptide binding, insertion, and membrane perturbation. These experiments yield critical data on membrane selectivity, peptide-induced pore formation, and the structural determinants of peptide-membrane affinity, informing the rational design of membrane-active agents.
Peptide engineering and analog development: Indolicidin serves as a foundational template in the field of peptide engineering, where its sequence is modified to explore structure-activity relationships and enhance functional attributes. Researchers synthesize derivatives and analogs by substituting specific residues, cyclizing the backbone, or introducing non-natural amino acids, aiming to improve potency, selectivity, or stability. Such studies not only expand the repertoire of antimicrobial peptides but also contribute to the development of novel biomolecules for diverse applications, including biofilm disruption and surface coatings.
Innate immunity and host-pathogen interaction studies: As a prototypical host defense peptide, indolicidin is employed in experimental models to investigate the cellular and molecular aspects of innate immune responses. Its interactions with microbial invaders, immune cells, and inflammatory mediators provide a platform for dissecting the role of endogenous peptides in pathogen clearance and immune modulation. Through in vitro and ex vivo assays, the peptide enables researchers to explore signaling pathways, cytokine release, and the cross-talk between innate and adaptive immunity, offering valuable perspectives on host-pathogen dynamics.
Analytical and assay development: The well-characterized sequence and robust activity profile of indolicidin make it a valuable reference standard in the development and validation of antimicrobial assays. It is frequently used as a positive control in microdilution, radial diffusion, and membrane leakage assays, ensuring assay reliability and comparability across laboratories. Additionally, its defined physicochemical properties facilitate the calibration of analytical techniques such as mass spectrometry and high-performance liquid chromatography, supporting accurate quantification and characterization of peptide samples in research and quality control settings.
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