, 2004); peptides that bind to specific targets in the Gefitinib research buy membranes of cancer cells, such as chlorotoxin from scorpion venom (Deshane et al., 2003) targeting metalloproteinases from glioma cells, leading to cell death (Mamelak and Jacoby, 2007);

angiogenesis inhibitors (Arbiser et al., 2007); toxins responsible for the permeabilization of cancer cell membranes (Saini et al., 1999); and others. Research regarding toxins has become a very exciting field to study because of the recent advances in genomic and proteomic technologies, such as the venomous systems genome project (Menez et al., 2006) and the development of methods to screen venoms and toxins (Escoubas, 2006b and Favreau et al., 2006), allowing better alternatives and means to study the pharmacologically active substances found so far. Venoms from these animals may hold the promises for curing many types of malignancies, especially upon analyzing results

from studies which show a complete remission of tumor cells after treatment with molecules derived from animal venom. However, studies focusing on the mechanism by which these venoms act are still very recent, and much has yet to be found out about these molecules. The first clinical trials against cancer using synthetic peptides derived from AZD9291 in vivo animal venom are beginning to show results; as more positive results are obtained, researchers and patients find reasons to believe that these small substances found in nature may have extraordinary applications. In this review, we will briefly describe some active principles from arthropod venoms that display activities against tumor cells. Scorpion venoms are a complex mixture of a large variety of molecules and they play an important role in the defense

and capture of prey. In contrast to spider and Thiamine-diphosphate kinase snake venoms, scorpion venom usually displays low levels of enzymatic activity (Gwee et al., 2002). They contain mucopolysaccarides, phospholipases, hyaluronidases, protease inhibitors, low molecular weight molecules such as serotonin and histamine, histamine releasing peptides, inorganic salts, mucus, and many basic small proteins called neurotoxic peptides (Martin-Eauclaire and Couraud, 1995, Müller, 1993 and Simard and Watt, 1990). The latter have specific interaction with ion channels, making scorpion venom capable of binding specifically to certain types of cells, such as cancer cells; therefore, this type of venom holds molecules that are of interest to the pharmaceutical industry in terms of drug design and development. Over 1500 scorpion species have been identified, each producing a different type of venom; each venom is estimated to be composed of 50–100 different toxic polypeptides (Lourenço, 1994 and Possani et al., 2000). Of these 1500 species, only a few dozen have been well studied.