LL-37, acetylated, amidated is a cathelicidin peptide LL-37 acetylated on the N-terminus and amidated on the C-terminus. The single human cathelicidin peptide LL-37 has antimicrobial and anti-biofilm activity against multiple Gram-positive and Gram-negative human pathogens, and has wound-healing effects on the host.
CAT No: R1487
LL-37, acetylated, amidated is a synthetic, chemically modified form of the human cathelicidin antimicrobial peptide LL-37, distinguished by N-terminal acetylation and C-terminal amidation. As a cationic, amphipathic peptide, LL-37 plays a vital role in the innate immune response, exhibiting broad-spectrum antimicrobial activity and modulating host cell signaling pathways. The acetylated and amidated modifications enhance its stability and bioactivity, making it a valuable tool for research into host defense mechanisms, peptide-membrane interactions, and immune modulation. Its unique properties position it at the forefront of studies exploring peptide-based regulation of microbial populations and cellular signaling cascades.
Antimicrobial peptide research: LL-37 analogs are extensively utilized in investigations of innate immunity and antimicrobial defense. The acetylated, amidated variant serves as a model for elucidating the mechanisms by which cationic peptides disrupt bacterial membranes, inhibit microbial growth, and exert selective activity against pathogens. Researchers employ this peptide to dissect structure-activity relationships, assess resistance mechanisms, and characterize the physicochemical determinants of antimicrobial efficacy. Such studies contribute to a deeper understanding of host-pathogen interactions and the development of novel antimicrobial strategies.
Membrane interaction studies: The amphipathic nature of LL-37 derivatives makes them ideal probes for examining peptide-lipid interactions and membrane dynamics. Scientists use the acetylated, amidated form to investigate how structural modifications influence peptide binding, insertion, and disruption of biological membranes. These studies are crucial for mapping the biophysical basis of peptide selectivity, cytotoxicity, and membrane remodeling, with implications for both fundamental biochemistry and the rational design of next-generation membrane-active agents.
Immunomodulation assays: Beyond direct antimicrobial effects, LL-37 variants are key tools in research on immunomodulatory signaling. The peptide is known to influence cytokine production, chemotaxis, and the activation of various immune cell types. By employing the acetylated, amidated version in cell-based assays, researchers can explore how post-translational modifications alter its capacity to modulate inflammatory responses, promote tissue repair, or regulate immune homeostasis. These insights are instrumental for advancing knowledge of immune regulation and peptide-based modulation of inflammation.
Peptide stability and protease resistance studies: Chemical modifications such as acetylation and amidation are frequently introduced to enhance peptide stability and resistance to proteolytic degradation. The modified LL-37 serves as a benchmark in experiments designed to compare degradation kinetics, assess half-life in biological fluids, and optimize peptide formulations for research use. Such applications are fundamental for understanding how structural changes affect peptide persistence and functionality in complex biological environments.
Peptide synthesis and analytical validation: The acetylated, amidated LL-37 is also employed as a reference standard in peptide synthesis optimization and analytical method development. Researchers utilize this compound to calibrate chromatographic systems, validate mass spectrometry protocols, and benchmark synthetic methodologies. Its defined structure and well-characterized properties support quality control processes and facilitate the accurate quantification and identification of cathelicidin peptides in experimental settings.
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