Open Access Research

Designed hybrid TPR peptide targeting Hsp90 as a novel anticancer agent

Tomohisa Horibe, Masayuki Kohno, Mari Haramoto, Koji Ohara and Koji Kawakami*

Author Affiliations

Department of Pharmacoepidemiology, Graduate School of Medicine and Public Health, Kyoto University, Yoshida Konoecho, Sakyo-ku, Kyoto, 606-8501, Japan

For all author emails, please log on.

Journal of Translational Medicine 2011, 9:8  doi:10.1186/1479-5876-9-8

Published: 14 January 2011

Additional files

Additional file 1:

Intracellular penetration of antennapedia helix III homeodomain (Antp)-conjugated Antp-TPR hybrid peptide. BXPC3 cells were incubated with 10 μM of carboxytetramethyl rhodamine (TAMRA)-labeled Antp-TPR (Antp-TPR-TAMRA) or TPR (TPR-TAMRA) as indicated. Cells were then analyzed by phase-contrast (DIC), fluorescence (TAMRA-red) or merge image (DIC and TAMRA-red). All images were taken using confocal laser scanning microscopy as described in Methods. All scale bars are 50 μm.

Format: TIFF Size: 758KB Download file

Open Data

Additional file 2:

Effect of heat shock or Antp-TPR peptide treatment on the expression levels of Hsp90 or Hsp70 protein in normal and cancer cells. (A) Western-blot analysis in normal and cancer cell lines (HEK293T, Caki-1, BXPC3, T47D, and A549) receiving heat shock. Cell extracts after 2 hr of heat shock treatment (43°C) were examined for the expression of Hsp90 and Hsp70 by Western-blot analysis using specific antibodies. (B) Expression levels of Hsp70 in the normal and cancer cell lines (HEK293T, Caki-1, BXPC3, T47D, and A549) treated with hybrid Antp-TPR peptide. Cell extracts after treatment with Antp-TPR peptide were examined for the expression of Hsp70 by Western-blot analysis using specific antibodies. β-actin was used as the loading control.

Format: TIFF Size: 175KB Download file

Open Data