Proteomic characterization of venom from Scorpio fuscus (Scorpiones: Scorpionidae) with perspectives for therapeutic applications

dc.contributor.authorÇelebioğlu, Hasan Ufuk
dc.contributor.authorKandir, Sinan
dc.contributor.authorGokcek-Sarac, Cigdem
dc.contributor.authorYagmur, Ersen Aydin
dc.contributor.authorSvensson, Birte
dc.contributor.authorKarakurt, Serdar
dc.contributor.authorÇelebioğlu, Hasan Ufuk
dc.date.accessioned2025-10-18T10:10:58Z
dc.date.created2025
dc.date.issued2025
dc.departmentFakülteler, Fen Fakültesi, Biyoteknoloji Bölümü
dc.description.abstractScorpion venom, renowned for its complexity and bioactivity, presents a fascinating landscape of molecules with diverse functionalities. This study delves into the intricate world of Scorpio fuscus venom proteins involving 1D gel-based proteomics followed by de novo protein identification employing LC-MS/MS. A total of 84 proteins were identified, unveiling a multifaceted composition with distinct functional categories. Notable entities include heteroscorpine-1, venom peptides (HtLKTx1-6, maurocalcin, opiscorpine-1 to 4), and phospholipase A2 hemilipin. These proteins exhibit potential applications in ion channel modulation and antimicrobial activity. Although some toxins show in vitro cytotoxicity, further in vivo investigations are needed to assess their true anticancer potential. The investigation highlights 16 potential antimicrobial peptides/proteins, including Con22 and opiscorpine-1. Additionally, 13 proteins related to lipid metabolism, such as phospholipase A2 heteromtoxin, were identified, suggesting potential effects in angiogenesis and cellular processes. The study identified the alpha KTx6.2 channel toxin peptide, maurotoxin, a potent inhibitor of voltage-dependent potassium channels. The presence of hemocyanin, a respiratory pigment, adds complexity to our insight into scorpion physiology, suggesting potential roles in immune responses and resistance to ionizing irradiations, beyond oxygen transport. Furthermore, the identification of proteins unknown or uncharacterized for their functions, including La1-like protein 13 and CAPUro-1, extends the intricacy of the venom composition, warranting further investigations into their functional significance. This comprehensive analysis provides a nuanced perspective on the Scorpio fuscus venom, shedding light on potential therapeutic avenues, antimicrobial applications, and the evolutionary adaptations that have shaped scorpion venoms.
dc.description.sponsorshipScientific and Technological Research Council of Turkiye (TUBITAK) [120Z942]; Selcuk University Research Foundation, Turkiye [21401070]
dc.description.sponsorshipThis study was supported by the Scientific and Technological Research Council of Turkiye (TUBITAK; Grant No. 120Z942) and Selcuk University Research Foundation, Turkiye (BAP, Grant No. 21401070).
dc.identifier.doi10.1016/j.toxicon.2025.108506
dc.identifier.issn0041-0101
dc.identifier.issn1879-3150
dc.identifier.orcidSvensson, Birte/0000-0002-2993-8196
dc.identifier.pmid40714116
dc.identifier.scopus2-s2.0-105011753400
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1016/j.toxicon.2025.108506
dc.identifier.urihttps://hdl.handle.net/11772/22134
dc.identifier.volume265
dc.identifier.wosWOS:001585440600002
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherPergamon-Elsevier Science Ltd
dc.relation.ispartofToxicon
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.relation.sdgGoal-03: Good Health and Well-Being
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzWoS_20251016
dc.subjectScorpio Fuscus
dc.subjectScorpion Venom
dc.subjectGel-Based Proteomics
dc.subjectLc-Ms/Ms
dc.subjectPotassium Channel Inhibitors
dc.subjectAntimicrobial Peptides
dc.subjectTherapeutic Peptides
dc.titleProteomic characterization of venom from Scorpio fuscus (Scorpiones: Scorpionidae) with perspectives for therapeutic applications
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublication5539ce82-066d-4ab0-a785-a3ce0f3c9369
relation.isAuthorOfPublication.latestForDiscovery5539ce82-066d-4ab0-a785-a3ce0f3c9369

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