Abstract
Spider venoms are complex mixtures of active molecules, including proteins, small peptides, and other organic compounds, such as polyamines. They have been investigated in drug discovery processes, and the number of patent applications comprising spider venoms, toxins, and derivatives in biotechnological inventions shows the various uses of these molecules. Spider peptide toxins are mainly active on ion channels and can be specific for insects (leading to the design of insecticides) as well as for mammals (enabling the design of drugs for the treatment of neurological diseases, pain, erectile dysfunction, or cancer). Some spider peptide toxins have been investigated for the development of antimicrobial drugs. Spider acylpolyamines have been investigated for the treatment of several neurodegenerative diseases. Patent applications comprising spider venom molecules from species of all continents have been filed in many countries, mostly in the USA, China, Germany, and Great Britain. Many species have been cited in these documents, being Loxosceles, Nephila, Atrax, Hadronyche, and Sicarius the most claimed genera. This chapter demonstrates that much effort has been made aiming at the development of new drugs based on the study of spider venom molecules, showing that spiders are a great source of natural molecules that can become valuable products in various fields, from agriculture to human therapy.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Adams ME. Agatoxins: ion channel specific toxins from the American funnel web spider, Agelenopsis aperta. Toxicon. 2004;43(5):509–25.
Beleboni RO, Carolino RO, Pizzo AB, Castellan-Baldan L, Coutinho-Netto J, dos Santos WF, Coimbra NC. Pharmacological and biochemical aspects of GABAergic neurotransmission: pathological and neuropsychobiological relationships. Cell Mol Neurobiol. 2004;24(6):707–28.
Cabbiness SG, Gehrke CW, Kuo KC, Chan TK, Hall JE, Hudiburg SA, Odell GV. Polyamines in some tarantula venoms. Toxicon. 1980;18(5–6):681–3.
Corzo G, Gilles N, Satake H, Villegas E, Dai L, Nakajima T, Haupt J. Distinct primary structures of the major peptide toxins from the venom of the spider Macrothele gigas that bind to sites 3 and 4 in the sodium channel. FEBS Lett. 2003;547:43–50.
Coutinho-Netto J, Abdul-Ghani AS, Collins JF, Bradford HF. Is glutamate a trigger factor in epileptic hyperactivity? Epilepsia. 1981;22(3):289–96.
Escoubas P, Sollod BL, King GF. Venom landscapes: mining the complexity of spider venoms via a combined cDNA and mass spectrometric approach. Toxicon. 2006;47:650–63.
Lazarev VN, Shkarupeta MM, Polina NF, Kostrjukova ES, Vassilevski AA, Kozlov SA, Grishin EV, Govorun VM. Antimicrobial peptide from spider venom inhibits Chlamydia trachomatis infection at an early stage. Arch Microbiol. 2013;195(3):173–9.
Olney JW. Excitotoxicity: an overview. Can Dis Wkly Rep. 1990;16(Suppl 1E):47–57.
Palagi A, Kohb JMS, Leblanca M, Wilsonc D, Dutertrec S, King GF, Nicholson GM, Escoubas P. Unravelling the complex venom landscapes of lethal Australian funnel-web spiders (Hexathelidae: Atracinae) using LC-MALDI-TOF mass spectrometry. J Proteomics. 2013;80:292–310.
Santos DM, Verly RM, Piló-Veloso D, de Maria M, de Carvalho MA, Cisalpino PS, Soares BM, Diniz CG, Farias LM, Moreira DF, Frézard F, Bemquerer MP, Pimenta AM, de Lima ME. LyeTx I, a potent antimicrobial peptide from the venom of the spider Lycosa erythrognatha. Amino Acids. 2010;39(1):135–44.
Siemens J, Zhou S, Piskorowski R, Nikai T, Lumpkin EA, Basbaum AI, King D, Julius D. Spider toxins activate the capsaicin receptor to produce inflammatory pain. Nature. 2006;444(7116):208–12.
Tan H, Ding X, Meng S, Liu C, Wang H, Xia L, Liu Z, Liang S. Antimicrobial potential of lycosin-I, a cationic and amphiphilic peptide from the venom of the spider Lycosa singorensis. Curr Mol Med. 2013;13(6):900–10.
Vajda FJ. Neuroprotection and neurodegenerative disease. J Clin Neurosci. 2002;9(1):4–8.
Vassilevski AA, Kozlov SA, Grishin EV. Molecular diversity of spider venom. Biochemistry (Mosc). 2009;74(13):1505–34.
Vetter I, Davis JL, Rash LD, Anangi R, Mobli M, Alewood PF, Lewis RJ, King GF. Venomics: a new paradigm for natural products-based drug discovery. Amino Acids. 2011;40:15–28.
Wan H, Lee KS, Kim BY, Zou FM, Yoon HJ, Je YH, Li J, Jin BR. A spider-derived Kunitz-type serine protease inhibitor that acts as a plasmin inhibitor and an elastase inhibitor. PLoS One. 2013;8(1):e53343.
Windley MJ, Herzig V, Dziemborowicz SA, Hardy MC, King GK, Nicholson GM. Spider-venom peptides as bioinsecticides. Toxins. 2012;4:191–227.
Xiong XF, Poulsen MH, Hussein RA, Nørager NG, Strømgaard K. Structure-activity relationship study of spider polyamine toxins as inhibitors of ionotropic glutamate receptors. ChemMedChem. 2014;9(12):2661–70.
Yan L, Adams ME. Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis. J Biol Chem. 1998;273(4):2059–66.
Zhou Y, Zhao M, Fields GB, Wu CF, Branton WD. δ/ω-Plectoxin-Pt1a: an excitatory spider toxin with actions on both Ca(2+) and Na(+) channels. PLoS One. 2013;8(5):e64324.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Science+Business Media Dordrecht
About this entry
Cite this entry
Matavel, A., Estrada, G., De Marco Almeida, F. (2016). Spider Venom and Drug Discovery: A Review. In: Gopalakrishnakone, P., Corzo, G., de Lima, M., Diego-García, E. (eds) Spider Venoms. Toxinology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6389-0_9
Download citation
DOI: https://doi.org/10.1007/978-94-007-6389-0_9
Published:
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-007-6388-3
Online ISBN: 978-94-007-6389-0
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences