Investigating the cytotoxic effects of the venom proteome of two species of the Viperidae family (Cerastes cerastes and Cryptelytrops purpureomaculatus) from various habitats

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dc.contributor.authorOzverel, Cenk Serhan
dc.contributor.authorDamm, Maik
dc.contributor.authorHempel, Benjamin-Florian
dc.contributor.authorGocmen, Bayram
dc.contributor.authorSroka, Robert
dc.contributor.authorSuessmuth, Roderich D.
dc.contributor.authorNalbantsoy, Ayse
dc.date.accessioned2019-10-27T09:43:59Z
dc.date.available2019-10-27T09:43:59Z
dc.date.issued2019
dc.departmentEge Üniversitesien_US
dc.description.abstractAnimal secretions are of great interest in terms of drug development due to their complex protein and peptide composition. Especially, in the field of therapeutic medications such as anti-cancer drugs snake venoms receive attention. In this study, we address two Viperidae species from various habitats with a particular focus on the cytotoxic potential along with the decomplexation of the venom proteome: the horned desert viper (Cerastes cerastes), native to desert regions of North Africa and the mangrove pit viper (Cryptelytrops purpureomaculatus), found in coastal forests of Southeast Asia. Initial cytotoxic screenings of the crude venoms revealed diverse activity, with the highest effect against SHSY5Y human glioblastoma carcinoma cells compared to other cancerous and non-cancerous cell lines. In-depth cytotoxicity studies of SHSY5Y cells with purified venom fractions revealed heterodimeric disintegrins from C. cerastes venom, which exerted a high cytotoxic activity with IC50 values from 0.11 to 0.58 mu M and a disintegrin-like effect on SHSY5Y morphology was observed due to cell detachment. Furthermore, two polyproline BPP-related peptides, one PLA(2) and a peptide-rich fraction were determined for C. purpureomaculatus with moderate IC50 values between 3 and 51 mu M. Additionally, the decryption of the venom proteomes by snake venomic mass spectrometry and comparison of the same species from different habitats revealed slight differences in the composition.en_US
dc.identifier.doi10.1016/j.cbpc.2019.02.013en_US
dc.identifier.endpage30en_US
dc.identifier.issn1532-0456
dc.identifier.issn1878-1659
dc.identifier.pmid30825636en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage20en_US
dc.identifier.urihttps://doi.org/10.1016/j.cbpc.2019.02.013
dc.identifier.urihttps://hdl.handle.net/11454/28942
dc.identifier.volume220en_US
dc.identifier.wosWOS:000469306000003en_US
dc.identifier.wosqualityQ1en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevier Science Incen_US
dc.relation.ispartofComparative Biochemistry and Physiology C-Toxicology & Pharmacologyen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectCerastes cerastesen_US
dc.subjectCryptelytrops purpureomaculatusen_US
dc.subjectCytotoxicityen_US
dc.subjectDisintegrinsen_US
dc.subjectPolyprolineen_US
dc.subjectSnake venomicsen_US
dc.subjectVenomen_US
dc.titleInvestigating the cytotoxic effects of the venom proteome of two species of the Viperidae family (Cerastes cerastes and Cryptelytrops purpureomaculatus) from various habitatsen_US
dc.typeArticleen_US

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