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_e _e _aConsul, Sarah Hannah Eynice G.; Ravalo, Antonio S.; Ronquillo, Kyle Kevin B.; Salva, Danielle Anne R,; Solasco, Raphaela Angela P. _d _b4 _u _c0 _q16 |
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_a _aCharacterization of toxic venom components of diadema setosum and its interaction with voltage-gated Ion channels _d _b _n _c _h6 _p |
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_b _atext _2rdacontent |
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_3 _30 _b _aunmediated _2rdamedia |
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_3 _30 _b _avolume _2rdacarrier |
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_a _aUndergraduate Thesis: (BS in Biology major in Cell and Molecular Biology) - Pamantasan ng Lungsod ng Maynila, 2024 _d _b _c56 |
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_b _b _c _aABSTRACT: Marine invertebrates, encompassing a vast array of creatures from sea stars to jellyfish, have evolved a remarkable arsenal of venoms for defense and predation. These venoms often contain a complex cocktail of bioactive molecules, including toxic enzymatic peptides and organic compounds, with the ability to target specific biological systems. Understanding the intricate workings of these venoms is not only crucial from a medical standpoint, for treating envenomations, but also holds significant scientific interest, potentially offering insights into novel drug development and physiological processes. This study aimed to identify and characterize the venom components of the sea urchin Diadema setosum, specifically focusing on their potential neurotoxic effects and its interaction to voltage-gated ion channels. Samples collected were dissected and analyzed using DNA extraction, PCR amplification, and in silico techniques. The analysis identified a lectin protein sequence in Diadema setosum venom. In silico docking simulations revealed preferential binding of this rhamnose-binding lectin (RBL) to voltage-gated sodium channels compared to potassium channels. This suggests a potential mechanism for Diadema setosum venom toxicity by targeting sodium channels, potentially contributing to neuronal inflammation. However, while these in silico simulations provide promising insights, further experimental validation is necessary to definitively confirm the predicted interactions and their biological significance. Overall, this study contributes to the understanding of the molecular basis of Diadema setosum venom toxicity and paves the way for future research into its potential effects on cellular function, alongside the continued exploration of other marine venoms and their complex mechanisms. Keywords: rhamnose-binding lectin, sea urchin, voltage-gated ion channels _u |
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