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 is a synthetic peptide fragment derived from the N-terminal region of human lactoferrin, a multifunctional glycoprotein found in various secretory fluids and neutrophil granules. As an 11-amino acid peptide, hLF1-11 is distinguished by its cationic nature and amphipathic structure, which underpin its notable bioactivity and relevance in biochemical research. Its sequence confers a unique ability to interact with microbial membranes and modulate host cellular responses, making it a valuable tool for studies focused on innate immunity, antimicrobial mechanisms, and peptide-membrane interactions. The robust scientific interest in hLF1-11 stems from its well-characterized structure-function relationships and its utility as a model peptide for exploring the diverse roles of lactoferrin-derived fragments in biological systems.
Antimicrobial mechanism studies: hLF1-11 serves as a prominent model in the investigation of antimicrobial peptide action. Researchers utilize it to elucidate the molecular mechanisms by which cationic peptides disrupt bacterial membranes, inhibit microbial growth, or neutralize pathogens. Its defined sequence and predictable folding properties allow for systematic studies on peptide-lipid interactions, membrane permeabilization, and the influence of peptide charge distribution on microbial susceptibility. These insights inform the broader understanding of host defense peptides and their potential as templates for new bioactive molecules.
Innate immune modulation research: The peptide is widely employed to study the modulation of innate immune responses, particularly in the context of neutrophil function and inflammatory signaling. Its interactions with immune cell receptors and its ability to influence cytokine production make it a valuable probe for dissecting the molecular pathways underlying immune activation and regulation. Such studies leverage hLF1-11 to clarify the contributions of lactoferrin-derived sequences to immune homeostasis and the resolution of infection-related inflammation.
Peptide-membrane interaction assays: Owing to its amphipathic and cationic properties, hLF1-11 is frequently used in biophysical and biochemical assays designed to characterize peptide-membrane interactions. Researchers employ it in lipid bilayer models, vesicle leakage experiments, and surface plasmon resonance studies to quantify binding affinities, membrane disruption kinetics, and structural changes upon peptide insertion. These assays provide critical data for understanding the determinants of peptide selectivity and potency against microbial versus host membranes.
Structure-activity relationship (SAR) analysis: The defined sequence of hLF1-11 makes it an ideal candidate for systematic structure-activity relationship studies. Scientists synthesize analogs with targeted substitutions or modifications to map the contribution of individual amino acid residues to biological activity. Such SAR analyses facilitate the identification of key structural motifs responsible for antimicrobial or immunomodulatory properties, guiding the rational design of optimized peptide derivatives for research applications.
Peptide synthesis and analytical method development: hLF1-11 is utilized as a reference peptide in the optimization of solid-phase peptide synthesis protocols and in the validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized nature and moderate length make it a practical standard for assessing peptide purity, yield, and sequence fidelity, supporting the development and quality control of peptide-based research tools and products.
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