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DNA Transfection Efficiency of Antimicrobial Peptide as Revealed by Molecular Dynamics Simulation

Published online by Cambridge University Press:  25 June 2013

Namsrai Javkhlantugs
Affiliation:
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 Department of Advanced Materials Science, Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai, Hodogaya ku, Yokohama 240-8501, Japan
Janlav Munkhtsetseg
Affiliation:
Department of Biochemistry and Laboratory, School of Biomedicine, Health Sciences University of Mongolia, Zorigiin gudamj, Ulaanbaatar 14210, Mongolia
Chimed Ganzorig
Affiliation:
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
Kazuyoshi Ueda
Affiliation:
Department of Advanced Materials Science, Graduate School of Engineering, Yokohama National University, 79-5 Tokiwadai, Hodogaya ku, Yokohama 240-8501, Japan
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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.

Type
Articles
Copyright
Copyright © Materials Research Society 2013 

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References

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