Impacts of carbon nanotubes on biochemical reactions: insight into interaction between carbon nanotubes and DNA polymerase enzyme
Uysal, Ebru and Meral, Yüce and Kurt, Hasan (2014) Impacts of carbon nanotubes on biochemical reactions: insight into interaction between carbon nanotubes and DNA polymerase enzyme. In: 16th European Congress on Biotechnology, Edinburgh, Scotland
Official URL: http://dx.doi.org/10.1016/j.nbt.2014.05.895
Recently, the Polymerase Chain Reaction technique has begun to benefit from nanotechnology. In this paper, effects of carbon nanotubes in the Polymerase Chain Reaction were investigated by Electrophoresis, Circular Dichroism Spectrometry and Dynamic Light Scattering Techniques. The unique ability to amplify low copy number DNA within minutes has made in vitro Polymerase Chain Reaction (PCR) one of the most essential techniques in modern biology. In order to harness this technique to its full potential, certain obstacles, such as nonspecific by-products, low yield, and complexity of GC rich and long genomic DNA amplification need to be surmounted. Nanomaterial-assisted PCR, so-called nanoPCR, is a new area in biotechnology that introduces nanostructured materials into PCR reaction to obtain improved results. Nanomaterials have unique physical and chemical properties, such as high thermal conductivity, stability and high surface to volume ratios. The effects of nanomaterials in PCR depend on their size, shape, concentration, heat conductivity, electron transfer properties and surface modifications. Carbon nanotubes are predicted to bind major PCR components, such as primers, template and polymerase enzyme, via specific or non-specific interactions. In this paper, we demonstrate the interaction of carbon nanotubes with wild type DNA polymerase enzyme, and the effect of this interaction in PCR for the first time. According to the results, chiral properties of the wild type DNApolymerase enzyme has changed after incubation with amine functionalized multiwall carbon nanotubes, which confirms direct interaction between the enzyme and tubes. Furthermore, this interaction has been found to be temperature dependent via dynamic light scattering spectroscopy.
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