Drug Discoveries & Therapeutics
Online ISSN : 1881-784X
Print ISSN : 1881-7831
ISSN-L : 1881-7831
Original Articles
Design of amphiphilic oligopeptides as models for fine tuning peptide assembly with plasmid DNA
Geetha N. GoparajuPardeep K. Gupta
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2014 Volume 8 Issue 4 Pages 165-172

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Abstract

We discuss the design of novel amphiphilic oligopeptides with hydrophobic and cationic amino acids to serve as models to understand peptide-DNA assembly. Biophysical and thermodynamic characterization of interaction of these amphiphilic peptides with plasmid DNA is presented. Peptides with at least +4 charges favor stable complex formation. Surface potential is dependent on the type of hydrophobic amino acid for a certain charge. Thermodynamically it is a spontaneous interaction between most of the peptides and plasmid DNA. Lys7 and Tyr peptides with +4/+5 charges indicate cooperative binding with pDNA without saturation of interaction while Val2-Gly-Lys4, Val-Gly-Lys5, and Phe-Gly-Lys5 lead to saturation of interaction indicating condensed pDNA within the range of N/Ps studied. We show that the biophysical properties of DNA-peptide complexes could be modulated by design and the peptides presented here could be used as building blocks for creating DNA-peptide complexes for various biomedical applications, mainly nucleic acid delivery.

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© 2014 International Research and Cooperation Association for Bio & Socio-Sciences Advancement
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