Binding mechanism of affinity ligands for purification of plasmid DNA

Forde, G.M., Ying, H., & (2007) Binding mechanism of affinity ligands for purification of plasmid DNA. In 2007 AIChE Annual Meeting, 4-9 November 2007, Salt Lake City, UT.

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Plasmid DNA for therapeutic and vaccination purposes must be highly purified. The high selectivity of affinity chromatography makes it ideal for the isolation of pDNA from complex biological feed stocks. Affinity chromatography makes use of the biological function and/or individual chemical structure of the interacting molecules. However, the success of any affinity purification protocol is dependent on the availability of suitable ligands. In this study, surface plasmon resonance (SPR) based Biacore system has been employed for the detection and quantification of the binding between lac operon (lacO) sequence contained in a pDNA and synthetic peptides based on the DNA-binding domain of the lac repressor protein, lad. The equilibrium dissociation constant (K D) and association and dissociation rate constants (ka, kd) for the interaction between plasmid DNA and designed peptides were determined.

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ID Code: 81559
Item Type: Conference Paper
Refereed: No
Keywords: Affinity chromatography, Amines, Chromatographic analysis, Chromatography, Dissociation, Genes, Ligands, Nucleic acids, Organic acids, Peptides, Proteins, Purification, Rate constants, Surface plasmon resonance, Affinity ligands, Affinity purifications, BIA cores, Binding mechanisms, Biological feeds, Biological functions, Chemical structures, Dissociation rate constants, Dna bindings, Equilibrium dissociation constants, High selectivities, Interacting molecules, Lac operons, Lac repressors, Plasmid dnas, Surface plasmons, Synthetic peptides, DNA
Divisions: Current > Schools > School of Chemistry, Physics & Mechanical Engineering
Current > QUT Faculties and Divisions > Science & Engineering Faculty
Deposited On: 05 Feb 2015 22:51
Last Modified: 11 Feb 2015 04:52

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