Institute of
bioorganic chemistry

Scientists from the Laboratory of Neuroreceptors and Neuroregulators of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, in collaboration with colleagues from the Institute of Experimental Chemical Physics named after. V.L. Talroze Federal Research Center for Chemical Physics of the Russian Academy of Sciences, using a combined approach of transcriptomics and proteomics, conducted a comprehensive analysis of the polypeptide composition of the venom of the Central Asian spider Tibellus oblongus. Based on analysis of the EST (Expressed Sequence Tags) database, the amino acid sequences of 345 precursor proteins and 217 mature toxins were determined. Using bottom-up proteomics, 212 natural toxins were detected in the venom sample and the post-translational modifications were confirmed. This is the first time that the primary structure has been determined simultaneously for numerous toxins from one spider species. Analysis of the primary structure indicated that some molecules have an ICK (inhibitor cystine knot) organization common for spider toxins, but a significant part of the toxins represents new structural motifs and have no homology with known peptides. The study was published in the Scientific Data.