Unless infection occurs, a slight inflammation at the puncture site can arise. Spiders of the family Theraphosidae have ALK inhibitor urticating hairs covering their bodies, which are brushed off by the spider as a mechanism of defense to deter predators. These hairs were found to induce local dermatitis in vertebrates, including humans ( Shrum et al., 1999). The puncture wounds from the spider’s fangs require local wound care, follow-up

for signs of infection, short-term analgesia and a tetanus booster ( Kelley and Wasserman, 1998; Shrum et al., 1999). The spider venom is a diverse mixture of low molecular mass compounds (16% of all compounds), acylpolyamines (11%), linear peptides (6%), cysteine-knotted mini-proteins (60%), neurotoxic www.selleckchem.com/products/fg-4592.html proteins (1%) and enzymes (6%) (Jackson and Parks, 1989; Kuhn-Nentwig et al., 2011). It is mainly used to paralyze prey and for defense, and contains toxins that affect the central or peripheral nervous systems. These neurotoxins have been identified mostly as acylpolyamines and peptides or proteins that act on membrane receptors or ion channels (see review Estrada et al., 2007). The acylpolyamine toxins

are low molecular mass compounds (<1 kDa) that appear to have evolved to specifically provoke rapid paralysis. Their complex structures are composed by a polyamine chain with a primary amino or a guanidine group at one end and an aromatic ring at the other. These compounds interact with multiple targets in the central and peripheral nervous systems of insects, and also in the CNS of mammals, whereas the main targets are ionotropic

glutamate and nicotinic acetylcholine receptors (Kawai et al., 1982; Herold and Yaksh, 1992; Bixel et al., 2001). Eight hundred curated sequences of protein toxins have been described for spider venom to date, among them approximately 20% corresponds to Theraphosidae spiders (available at ArachnoServer 2.0; Herzig et al., 2011). Most of these 200 peptides has 30–40 amino Gefitinib acid residues, three disulfide bridges and basic character (Escoubas and Rash, 2004), and are modulators of ion-channels, such as calcium, sodium, and potassium. In this communication we report the results of proteomic and pharmacological characterizations of the venom extracted from the Brazilian spider Acanthoscurria paulensis. A. paulensis (Theraphosidae, Mygalomorphae) is a dark brown colored spider widely distributed in three Brazilian regions: South, Southeast and Midwest ( Mello-Leitão, 1923; Lucas et al., 2010).