LAH4 is an antimicrobial peptide that strongly interacts with phospholipid membranes, exhibiting in vitro transfection efficiency.
CAT No: R1474
LAH4 is a synthetic amphipathic peptide recognized for its unique ability to interact with biological membranes and facilitate the delivery of nucleic acids and other macromolecules into cells. Structurally engineered to adopt an alpha-helical conformation under physiological conditions, LAH4 exhibits pH-dependent membrane activity, making it a valuable tool in the study of membrane translocation mechanisms. Its distinctive sequence and physicochemical properties have positioned it as a model peptide for investigating cellular uptake processes, endosomal escape, and the modulation of lipid bilayers. Researchers in molecular biology, biochemistry, and pharmaceutical sciences have increasingly utilized LAH4 to address challenges related to intracellular delivery and membrane dynamics.
Gene delivery research: LAH4 has been extensively utilized as a non-viral vector for gene transfection studies in vitro. Its cationic nature and amphipathic design enable efficient binding to nucleic acids, such as DNA and RNA, forming stable complexes that can traverse cellular membranes. The peptide's ability to destabilize lipid bilayers at acidic pH, commonly encountered in endosomal compartments, facilitates endosomal escape and enhances transfection efficiency. As a result, LAH4 serves as a critical component in the development and optimization of peptide-based gene delivery systems, providing a versatile platform for advancing nucleic acid therapeutics research.
Membrane biophysics studies: In the field of membrane biophysics, LAH4 is employed as a model system to elucidate the mechanisms of peptide-membrane interactions. Its well-characterized structural transitions and membrane-perturbing activity allow researchers to investigate the factors influencing membrane permeability, peptide insertion, and lipid reorganization. By using LAH4 in model membrane systems, such as lipid vesicles or supported bilayers, scientists gain insights into the fundamental principles governing membrane-active peptides, which inform the design of novel biomimetic materials and drug delivery vehicles.
Intracellular delivery of macromolecules: Beyond nucleic acids, LAH4 has demonstrated utility in facilitating the cytosolic delivery of a diverse array of macromolecular cargos, including proteins, peptides, and small molecules. Its ability to promote endosomal escape and transiently disrupt membrane integrity under acidic conditions is harnessed to improve the intracellular availability of otherwise impermeable compounds. This application is particularly valuable in the context of functional studies requiring the introduction of bioactive agents into living cells for mechanistic investigations or high-content screening.
Antimicrobial peptide research: LAH4 is also investigated as a prototype antimicrobial peptide due to its membrane-disruptive properties. Studies leveraging its amphipathic structure and cationic charge profile have explored its interactions with bacterial membranes, providing insights into the design of novel antimicrobial agents. By analyzing the structure-activity relationships of LAH4 and its analogues, researchers aim to develop new strategies for combating microbial resistance and enhancing the efficacy of peptide-based antimicrobials.
Peptide engineering and structure-activity relationship (SAR) analysis: The modular nature of LAH4 makes it an ideal candidate for peptide engineering and SAR studies. Researchers frequently modify the sequence or structural features of LAH4 to probe the effects of specific amino acid substitutions, charge distribution, or hydrophobicity on membrane activity and cargo delivery. These systematic investigations contribute to a deeper understanding of the biophysical determinants of peptide function and support the rational design of next-generation delivery vectors and membrane-active therapeutics.
3. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
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