LL-37 (Human) Biotinylated, Pegylated combines the full-length human cathelicidin with PEG and biotin tags for enhanced solubility and affinity capture. The PEG segment modulates aggregation and diffusion, while biotin enables streptavidin-based immobilization. Researchers track its interactions with membranes, proteins, or nucleic acids. Applications include antimicrobial-peptide mechanism studies, binding assays, and surface-functionalization work.
CAT No: R2746
LL 37 (human) biotinylated, pegylated is a specialized synthetic peptide derived from the human cathelicidin antimicrobial peptide LL-37, uniquely modified through both biotinylation and pegylation. The biotinylation facilitates robust and specific binding to avidin or streptavidin-conjugated surfaces, enabling a range of downstream applications in detection, purification, and immobilization. Pegylation, the covalent attachment of polyethylene glycol (PEG) chains, enhances solubility, stability, and bioavailability, while reducing aggregation and nonspecific interactions. These dual modifications preserve the functional integrity of LL-37's active sequence, while providing superior handling characteristics for advanced research settings. The combination of these chemical modifications makes this peptide a versatile tool for researchers investigating innate immunity, peptide-membrane interactions, and biomolecular engineering, opening new avenues for both qualitative and quantitative studies in molecular biology.
Antimicrobial Mechanism Studies: LL 37 (human) biotinylated, pegylated serves as a powerful probe for dissecting the antimicrobial mechanisms of cathelicidin peptides. Its biotin tag allows for precise immobilization on biosensor chips or microtiter plates, enabling real-time interaction studies with bacterial membranes, lipopolysaccharides, or isolated microbial components. Researchers can use surface plasmon resonance (SPR), biolayer interferometry, or enzyme-linked detection platforms to quantitatively monitor binding events, conformational changes, and peptide-induced membrane disruptions. The pegylation ensures the peptide remains soluble and active throughout these assays, minimizing background noise and aggregation, thus providing clearer insights into the peptide's bactericidal action.
Host-Pathogen Interaction Analysis: In host-pathogen interaction studies, the biotinylated and pegylated LL-37 variant enables selective capture and visualization of peptide interactions with both human cells and microbial invaders. By anchoring the peptide to streptavidin-coated beads or surfaces, researchers can pull down binding partners from complex biological mixtures, facilitating identification of LL-37's cellular receptors, co-factors, or microbial evasion molecules. Pegylation further reduces nonspecific protein-protein interactions, improving the specificity of immunoprecipitation or affinity purification experiments. This approach supports the elucidation of molecular pathways involved in innate immune defense and microbial pathogenesis.
Peptide Structure-Function Relationship Investigations: The modified LL 37 peptide is invaluable for structure-function analyses, particularly when exploring the impact of chemical modifications on peptide activity. By comparing the behavior of biotinylated, pegylated LL-37 with its unmodified counterpart, scientists can assess how these modifications influence membrane binding, secondary structure, and resistance to proteolytic degradation. Techniques such as circular dichroism spectroscopy, fluorescence resonance energy transfer (FRET), and atomic force microscopy can be employed, leveraging the biotin tag for site-specific labeling or immobilization. Such studies deepen the understanding of how structural features govern the peptide's biological roles.
High-Throughput Screening Platforms: Biotinylated, pegylated LL-37 is well-suited for integration into high-throughput screening assays aimed at identifying modulators of antimicrobial activity or inhibitors of peptide-receptor interactions. Its stable, monodisperse nature allows for consistent coating of assay plates or biosensor arrays, enabling reproducible, automated workflows. The biotin-streptavidin system ensures strong, oriented attachment, while pegylation maintains peptide solubility even at high concentrations. This facilitates the rapid evaluation of chemical libraries, antibody candidates, or small molecules for their effects on LL-37 function, accelerating the discovery of new modulatory agents.
Immunoassay and Detection System Development: The dual modifications of LL 37 (human) biotinylated, pegylated make it an excellent standard or capture reagent in the development of immunoassays and biosensors. Its biotinylation allows for straightforward conjugation to detection platforms, while pegylation minimizes background interference and enhances assay sensitivity. Researchers can use it to create ELISA standards, calibrators, or as a capture agent in multiplexed detection systems, supporting the quantification of LL-37 levels in biological samples or the monitoring of peptide-based therapeutics in experimental models. These capabilities highlight the product's versatility and value in advancing both fundamental and applied peptide research.
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