Binding properties of peptidic affinity ligands for plasmid DNA capture and detection

Han, Ying, Gras, Sally, & Forde, Gareth M. (2009) Binding properties of peptidic affinity ligands for plasmid DNA capture and detection. AIChE Journal, 55(2), pp. 505-515.

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Abstract

Peptides constructed from α-helical subunits of the Lac repressor protein (LacI) were designed then tailored to achieve particular binding kinetics and dissociation constants for plasmid DNA purification and detection. Surface plasmon resonance was employed for quantification and characterization of the binding of double stranded Escherichia coli plasmid DNA (pUC19) via the lac operon (lacO) to "biomimics" of the DNA binding domain of LacI. Equilibrium dissociation constants (K D), association (k a), and dissociation rates (k d) for the interaction between a suite of peptide sequences and pUC19 were determined. K D values measured for the binding of pUC19 to the 47mer, 27mer, 16mer, and 14mer peptides were 8.8 ± 1.3 × 10 -10 M, 7.2 ± 0.6 × 10 -10 M, 4.5 ± 0.5 × 10 -8 M, and 6.2 ± 0.9 × 10 -6 M, respectively. These findings show that affinity peptides, composed of subunits from a naturally occurring operon-repressor interaction, can be designed to achieve binding characteristics suitable for affinity chromatography and biosensor devices.

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ID Code: 81541
Item Type: Journal Article
Refereed: Yes
Keywords: Binding kinetics, Peptide ligand design, Protein-nucleic acid interactions, Surface plasmon resonance, Synthetic peptide, Affinity ligands, Affinity peptides, Binding characteristics, Binding properties, Dissociation constants, Dissociation rates, Dna binding domains, Equilibrium dissociation constants, Lac operons, Lac repressors, Peptide sequences, Plasmid dnas, Affinity chromatography, Binding energy, Biosensors, Chromatographic analysis, Dissociation, DNA, Equilibrium constants, Escherichia coli, Genes, Ligands, Nucleic acids, Peptides, Plasmons, Amines
DOI: 10.1002/aic.11690
ISSN: 0001-1541
Divisions: Current > Schools > School of Chemistry, Physics & Mechanical Engineering
Current > QUT Faculties and Divisions > Science & Engineering Faculty
Deposited On: 05 Feb 2015 22:59
Last Modified: 11 Feb 2015 03:12

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