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Preparation of 125

  • Kim, Byoung-Soo (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Kim, Eun-Jung (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Lee, Hae-June (Laboratory of Radiation Effects, Korea Institute of Radiological and Medical Sciences) ;
  • Han, Sang-Jin (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Choi, Tae-Hyun (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Lee, Yun-Sil (Laboratory of Radiation Effects, Korea Institute of Radiological and Medical Sciences) ;
  • Cheon, Gi-Jeong (Department of Nuclear Medicine, Korea Institute of Radiological and Medical Sciences)
  • Received : 2010.06.17
  • Accepted : 2010.07.26
  • Published : 2010.09.20

Abstract

$PKC{\delta}$-catalytic V5 Heptapeptide (FEQFLDI, FP7) interacts with heat shock protein 27 (HSP27) and inhibits HSP27-mediated resistance to cell death against various stimuli including radiation therapy. Here, we prepared radio-iodinated heptapeptide and further investigated its uptake properties in HSP27 expression cells. Peptide sequence of FP7 and a negative control peptide (WSLLEKR, QP7) was modified by substituting their C-terminus residue to tyrosine (FP6Y and QP6Y) to label radio-iodine. Iodinated peptides were confirmed by LC mass analysis with cold iodine reaction mixture. Accumulation of [$^{125}I$]iodo-FP6Y and [$^{125}I$]iodo-QP6Y in NCI-H1299 cell line, with higher level of HSP27, and NCI-H460 cell line, with lower level of HSP27, was measured by NaI(Tl) scintillation counter. The modification of substituting C-terminus residue of FP7 to tyrosine (FP6Y) did not affect its interaction with HSP27. Accumulation of [$^{125}I$]iodo-FP6Y in NCI-H1299 cells was 3 fold higher than in NCI-H460 cells. The novel radio-iodinated FP6Y would be used as a tracer for targeting HSP27 protein.

Keywords

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