hLF1-11 is a synthetic peptide corresponding to the first 11 N-terminal amino acids of human lactoferrin (hLF1-11) with potential antimicrobial activity. hLF1-11 is effective against a variety of bacteria and fungi, including multidrug-resistant (MDR) strains of Acinetobacter baumannii and Staphylococcus aureus, and fluconazole-resistant Candida albicans strains.
CAT No: 10-101-148
Chemical Name:(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[(2-aminoacetyl)amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-hydroxypropanoyl]amino]-3-methylbutanoyl]amino]-5-oxopentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-3-sulfanylpropanoyl]amino]propanoic acid
hLF1-11, a synthetic peptide derived from the N-terminal region of human lactoferrin, is recognized for its distinctive cationic and amphipathic properties. This peptide is engineered to mimic the natural defense mechanisms of lactoferrin, a multifunctional glycoprotein found in various secretory fluids and neutrophil granules. The structural integrity of hLF1-11 enables it to interact efficiently with microbial membranes, conferring notable bioactivity in diverse biological environments. Due to its stability and ease of synthesis, hLF1-11 is widely utilized in research settings to investigate host-pathogen interactions, innate immune responses, and the modulation of inflammatory processes. Its unique sequence and physicochemical characteristics make it a valuable tool for probing molecular mechanisms in both in vitro and in vivo experimental systems.
Antimicrobial Research: hLF1-11 is extensively applied in the study of antimicrobial mechanisms, particularly for its ability to disrupt bacterial and fungal cell membranes. Researchers employ this peptide to examine how cationic peptides interact with microbial surfaces, leading to membrane permeabilization and cell death. Studies often utilize hLF1-11 to model the action of endogenous antimicrobial peptides, providing insights into the development of novel antimicrobial agents and strategies to combat resistant strains. By serving as a model compound, it supports the exploration of peptide-based alternatives to conventional antimicrobials, with a focus on understanding structure-activity relationships and optimizing peptide design for enhanced efficacy.
Innate Immunity Modulation: The peptide is a valuable asset in immunology research, where it is used to investigate the modulation of innate immune responses. hLF1-11 has been shown to influence the activation and recruitment of immune cells, including monocytes and neutrophils. Through in vitro assays, scientists explore its capacity to induce cytokine production and enhance phagocytic activity, thereby elucidating the signaling pathways and cellular interactions involved in early host defense. These findings contribute to a broader understanding of how host-derived peptides can be harnessed to modulate immune functions and potentially address immune dysregulation in various experimental models.
Biofilm Inhibition Studies: The ability of hLF1-11 to interfere with biofilm formation is of particular interest in microbiology research. Biofilms, which are complex communities of microorganisms encased in a protective matrix, present significant challenges in both clinical and industrial settings due to their resistance to conventional treatments. Investigations utilizing hLF1-11 focus on its capacity to disrupt biofilm integrity, prevent microbial adhesion, and reduce the viability of sessile cells. Such studies are instrumental in identifying new approaches to manage biofilm-associated problems, including persistent infections and biofouling of medical devices or industrial equipment.
Inflammatory Response Regulation: hLF1-11 is also employed in research focused on the regulation of inflammatory responses. Its interaction with immune cells and signaling molecules provides a platform for studying the mechanisms underlying inflammation and tissue homeostasis. Scientists use this peptide to assess its effects on the expression of pro-inflammatory and anti-inflammatory mediators in various cell types and animal models. These investigations help clarify the dual role of antimicrobial peptides in both direct pathogen elimination and the fine-tuning of host inflammatory pathways, offering valuable perspectives for the development of immunomodulatory agents.
Wound Healing and Tissue Regeneration: In the context of tissue repair, hLF1-11 is investigated for its potential to promote wound healing and support tissue regeneration. Experimental models often utilize it to assess its effects on cell migration, proliferation, and extracellular matrix remodeling. The peptide's ability to modulate the local immune environment and inhibit microbial colonization further enhances its relevance in studies aimed at understanding the interplay between antimicrobial activity and regenerative processes. Insights gained from these applications inform the design of peptide-based solutions for improving tissue repair and managing infection-related complications in diverse experimental systems.
Overall, hLF1-11 stands out as a multifunctional peptide with broad research utility across several scientific fields. Its applications in antimicrobial research, innate immunity modulation, biofilm inhibition, inflammatory response regulation, and wound healing provide a robust framework for advancing our understanding of host defense mechanisms and the development of innovative therapeutic strategies. As new research continues to uncover the molecular intricacies of hLF1-11, its value as a versatile tool in experimental biology and peptide science is further solidified, supporting a wide range of investigations into microbial pathogenesis, immune regulation, and tissue dynamics.
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