DNA Transfection Efficiency of Antimicrobial Peptide as Revealed by Molecular Dynamics Simulation
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DNA Transfection Efficiency of Antimicrobial Peptide as Revealed by Molecular Dynamics Simulation Namsrai Javkhlantugs1, 2, Janlav Munkhtsetseg3, Chimed Ganzorig1, and Kazuyoshi Ueda2 1
Center for Nanoscience and Nanotechnology & Department of Chemical Technology, School of Chemistry and Chemical Engineering, National University of Mongolia, Main building, University street 1, Ulaanbaatar 14201, Mongolia 2 Department of Advanced Materials Science, Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai, Hodogaya ku, Yokohama 240-8501, Japan 3 Department of Biochemistry and Laboratory, School of Biomedicine, Health Sciences University of Mongolia, Zorigiin gudamj, Ulaanbaatar 14210, Mongolia ABSTRACT The peptide-DNA complex was investigated by using molecular dynamics simulation to analyze the transfection efficiency of cationic amphipathic peptide. Previously, the cationic peptide, LFampinB, with positively charged amino acid residues of Lysines was used to investigate the orientation and interaction energies for entering the cell though disruption of the endosomal membrane. The same interactions were obtained for N-terminus of the LFampinB peptide with membrane and with plasmid DNA. The N-terminus of LFampinB can bind at minor groove of DNA to make complexation of the peptide with DNA. INTRODUCTION The investigations of the efficiency of DNA-transfection to eukaryotic cells are important as a basic research in potential applications of gene delivery. Cationic peptides with positively charged amino acid residues can bind to polyanionic DNA to form complexes with a net positive charge which can enter the cell through disruption of the endosomal membrane. One of such peptide is bovine lactoferrampin (LFampinB) which has strong antimicrobial activity and kills a wide variety of Candida albicans yeast and a number of bacteria such as Escherichia coli. This peptide was found in bovine lactoferrin and corresponding to 268-284 amino acid residues in the protein [1]. Solid-state nuclear magnetic resonance (ssNMR) method with 13C chemical shift oscillation analysis and molecular dynamics (MD) simulation were performed to reveal the local structure and orientation of LFampinB in the molecular level with mimetic bacterial membrane [2]. The interactions and the dynamic structure of LFampinB in mimetic bacterial membranes were demonstrated by ssNMR and MD simulation. LFampinB specifically interacted with acidic phospholipids in bacterial membranes. LFampinB may kill bacteria by causing leakage of potassium ions from the cell membranes and breaking off the concentration gradient across the
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cell membrane as revealed by quartz crystal microbalance and ion selective electrode measurements [2]. In this work, we investigated the interactions of LFampinB with DNA to reveal the DNA transfection efficiency. MATERIALS AND METHODS Construction of peptide and DNA LFampinB is a cationic amphipathic peptide which consists of 17 amino acid residues with a sequence of Trp-Lys-Leu-Leu-Ser-Lys-Ala-Gln-Glu-Lys-Phe-Gly-
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