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

Biologicals. 2009 Aug;37(4):222-9. doi: 10.1016/j.biologicals.2009.01.010. Epub 2009 Mar 4.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antineoplastic Agents / chemical synthesis*
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / pharmacology*
  • Antineoplastic Agents / therapeutic use
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / pharmacology
  • Crotalid Venoms / therapeutic use
  • Drug Evaluation, Preclinical
  • Humans
  • Jurkat Cells
  • Lysine / chemistry
  • Male
  • Melanoma, Experimental / pathology
  • Mice
  • Mice, Inbred BALB C
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / pharmacology*
  • Peptide Fragments / therapeutic use
  • Phospholipases A2 / chemistry
  • Protein Engineering
  • Protein Structure, Tertiary / physiology
  • Snake Venoms / chemistry
  • Snake Venoms / pharmacology*
  • Tumor Cells, Cultured

Substances

  • Antineoplastic Agents
  • Crotalid Venoms
  • Peptide Fragments
  • Snake Venoms
  • bothropstoxin
  • Phospholipases A2
  • Lysine