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Waleed Ahmed El-Said,Cheol-Heon Yea,Hyunhee Kim,최정우 한국물리학회 2009 Current Applied Physics Vol.9 No.2
HepG2 cells have been immobilized on nanoscale self-assembled synthetic oligopeptide modified chip surface and subsequently used for anticancer drug screening. Nanoscale controlled self-assembled peptide layer was investigated by AFM (Atomic Force Microscopy). The immobilization of HepG2 cells on nanoscale controlled surface was investigated by using Raman spectroscopy. HepG2 cells were grown on peptide modified gold surface acting as working electrode. The AFM investigation of the oligopeptide modified surface showed excellent agreement with the nanoscale nature of the peptide modification, and the voltammetric response of HepG2 cells on this surface towards an anticancer drug showed a linear relationship with the cell number. As an application, electrochemical detection of anticancer drug effect of HepG2 cells was shown. These results indicate that RGD (Arg-Gly-Asp) peptide self-assembled layer mediated the cell immobilization technique and the voltammetric signal analysis system can be applied to construct a cell chip for diagnosis, drug detection, and on-site monitoring. HepG2 cells have been immobilized on nanoscale self-assembled synthetic oligopeptide modified chip surface and subsequently used for anticancer drug screening. Nanoscale controlled self-assembled peptide layer was investigated by AFM (Atomic Force Microscopy). The immobilization of HepG2 cells on nanoscale controlled surface was investigated by using Raman spectroscopy. HepG2 cells were grown on peptide modified gold surface acting as working electrode. The AFM investigation of the oligopeptide modified surface showed excellent agreement with the nanoscale nature of the peptide modification, and the voltammetric response of HepG2 cells on this surface towards an anticancer drug showed a linear relationship with the cell number. As an application, electrochemical detection of anticancer drug effect of HepG2 cells was shown. These results indicate that RGD (Arg-Gly-Asp) peptide self-assembled layer mediated the cell immobilization technique and the voltammetric signal analysis system can be applied to construct a cell chip for diagnosis, drug detection, and on-site monitoring.
최정우,김상욱,Young Jun Kim,Cheol-Heon Yea,민준홍 한국화학공학회 2008 Korean Journal of Chemical Engineering Vol.25 No.5
A novel immobilization method of blue copper protein azurin on a gold surface was developed without a chemical linker using recombinant technique. Azurin was recombined with a cysteine anchors by site-directed mutagenesis (SDM) and used to effect the mutations, changing the codon for Leu39Cys (L39C) from CTG to TGC. The immobilization of the functionalized protein is confirmed by surface plasmon resonance (SPR) and its surface morphology is analyzed by scanning tunneling microscopy (STM). The immobilization efficiency has been increased about 76.3%, as compared to that of wild type azurin. The electrochemical property of the fabricated thin film was investigated by cyclic voltammetry (CV). As a result, cysteine-modified azurin can be used for making high quality protein film, and applied to the fabrication of nano-scale bioelectronics.