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Analysis of biomolecular specific interaction by Localized Surface Plasmon Resonance biosensor

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영어

The tumor suppressor protein p53 plays important role in disturbing the growth of cancer. The damage of p53 function, which results almost every from mutations within the DNA binding domain, is related with human cancers. When the metallic nano-particles are excited by light, free electrons will be polarized by the electric field of the incoming light. As a result, the collective electrons of the nanometer-sized metallic structures oscillate with the incident photon frequency which is denoted as a localized surface plasmon resonance(LSPR). An λmax shift will occur in each step and we expect the delta maxs to be different according to the different types of p53. As a results, between the promoter and p53 proteins affinity difference. The case of wild type, the mutation type is higher than the binding affinity. Also depending on the mutation, affinity appears differently. This result successfully explain a non-labeling detection system for biomolecular interaction and it possesses a remarkable potential as a sensitive, on-chip and multiplexing detection.

저자정보

  • Ho Jun JEON Dept. of chemical &biological engineering, Korea University, Seoul, 136-701.
  • Sang Jun SIM Dept. of chemical &biological engineering, Korea University, Seoul, 136-701.

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