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      Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy.

      Cancer research

      Transfection, Protein Structure, Tertiary, pharmacology, genetics, chemistry, Peptides, methods, Molecular Targeted Therapy, Mice, Inbred C57BL, Mice, drug therapy, Melanoma, Experimental, Humans, HeLa Cells, metabolism, antagonists & inhibitors, HSP70 Heat-Shock Proteins, Aptamers, Peptide, drug effects, Apoptosis, Antineoplastic Agents, Animals, Rats

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          Abstract

          The inhibition of heat shock protein 70 (HSP70) is an emerging strategy in cancer therapy. Unfortunately, no specific inhibitors are clinically available. By yeast two-hybrid screening, we have identified multiple peptide aptamers that bind HSP70. When expressed in human tumor cells, two among these peptide aptamers-A8 and A17-which bind to the peptide-binding and the ATP-binding domains of HSP70, respectively, specifically inhibited the chaperone activity, thereby increasing the cells' sensitivity to apoptosis induced by anticancer drugs. The 13-amino acid peptide from the variable region of A17 (called P17) retained the ability to specifically inhibit HSP70 and induced the regression of subcutaneous tumors in vivo after local or systemic injection. This antitumor effect was associated with an important recruitment of macrophages and T lymphocytes into the tumor bed. Altogether, these data indicate that peptide aptamers or peptides that target HSP70 may be considered as novel lead compounds for cancer therapy. © 2011 AACR.

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          Author and article information

          Journal
          10.1158/0008-5472.CAN-10-1443
          21224349

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