The ability to subdue relatively large targets without the assistance of webs implies the necessity of physical strength and effective venoms that should be able to act rapidly upon the victim. Theraphosids are distributed across the globe, occurring in various habitats. It has been previously postulated that the variety of ecological niches and predatory behaviors correlate with the pharmacological and molecular diversity of their venoms (Escoubas and Rash, 2004). The theraphosid venom is a complex mixture of salts, nucleotides, free aminoacids, neurotransmitters,

polyamines, peptides, Alectinib nmr proteins and enzymes (Escoubas et al., 2000; Escoubas and Rash, 2004; Rash and Hodgson, 2002; Savel-Niemann, 1989). The peptide mass mapping by MALDI-TOF MS of the venom of 55 tarantula species revealed a bimodal distribution of peptide molecular masses: 57.8% of the detected peptides have masses ranging from 3500 to 4500 Da, and 6.9% have masses ranging from 6500 to 7000 Da (Escoubas and Rash, 2004). http://www.selleckchem.com/products/BAY-73-4506.html Due to the potential biotechnological application of theraphosid venom components, intense toxinological investigations have been performed. By contrast, studies dedicated to the identification and structural and pharmacological characterization of peptides and other components of the venom of the theraphosid genus Acanthoscurria

are still lacking. The genus Acanthoscurria possesses 34 described species broadly distributed across the Neotropical region, especially in South America ( Lucas et al., 2011). Studies dedicated to the characterization of biologically active molecules from Acanthoscurria have been restricted to the investigation of antimicrobial peptides and polyamines present in the hemolymph of Acanthoscurria gomesiana ( Barbosa et al., 2007; Fazio et al., 2007, 2006; Lorenzini

et al., 2003a, b; Miranda et al., 2009; Moreira et al., 2007; Pereira et al., 2007; Remuzgo et al., 2008; Silva et al., 2000). The present study reports the purification, primary structure determination and electrophysiological effects on cockroach dorsal unpaired median (DUM) neurons of an anti-insect toxin, named μ-theraphotoxin-An1a (μ-TRTX-An1a, according to the ID-8 nomenclature proposed by King et al. 2008),1 from the venom of Acanthoscurria natalensis – a tarantula species occurring in the Brazilian biomes caatinga and cerrado. Adult female A. natalensis specimens, collected in the vicinities of Feira de Santana (Bahia, Brazil), were kept in captivity and subjected to multiple venom extraction procedures. Venom samples were extracted by electrical stimulation on the base of the chelicerae and were collected with a micropipette tip. The venom samples were then transferred to chilled acidified water (0.1% aqueous trifluoroacetic acid) and centrifuged to remove cellular debris and mucus. The supernatant fractions was lyophilized, pooled and stored at −20 °C until required. μ-TRTX-An1a was purified by two- or one-dimensional chromatography, as described below.