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      Antitumor effects of snake venom chemically modified Lys49 phospholipase A2-like BthTX-I and a synthetic peptide derived from its C-terminal region.

      Biologicals : journal of the International Association of Biological Standardization
      Animals, Antineoplastic Agents, chemical synthesis, chemistry, pharmacology, therapeutic use, Crotalid Venoms, Drug Evaluation, Preclinical, Humans, Jurkat Cells, Lysine, Male, Melanoma, Experimental, pathology, Mice, Mice, Inbred BALB C, Peptide Fragments, Phospholipases A2, Protein Engineering, Protein Structure, Tertiary, physiology, Snake Venoms, Tumor Cells, Cultured

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          Abstract

          The present work evaluates both in vitro and in vivo antitumor activity of BPB-modified BthTX-I and its cationic synthetic peptide derived from the 115-129 C-terminal region. BPB-BthTX-I presented cytotoxicity of 10-40% on different tumor cell lines, which were also susceptible to the lytic action of the synthetic peptide. Injection of the modified protein or the peptide in mice, 5 days after transplantation of S180 tumor cells, reduced 30 and 36% of the tumor size on day 14th and 76 and 79% on day 60th, respectively, when compared to the untreated control group. Thus, these antitumor properties might be of interest in the development of therapeutic strategies against cancer.

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