Protein structure of the venom in nine species of snake: from bio-compounds to possible healing agents

Due to its various structures in bio-compounds, snake venom is the indisputable result of evolutionary stages of molecules with an increasingly complex structure, high specificity, and of great importance for medicine because of their potential. The present study proposed an underpinning examination of venom composition from nine species of venomous snakes using a useful and replicable methodology. The objective was the extension of the evaluation of protein fractions in the field up to 230 kDa to permit possible identification of some fractions that are insufficiently studied. The gel capillary electrophoresis method on the chip was performed using an Agilent 2100 bioassay with the 80 and 230-LabChip Protein kits. Interpretation of electrophoresis was performed using the Protein 2100 expert (Agilent) test software as follows: a) Protein 80 (peak size scale): 1.60, 3.5, 6.50, 15.00, 28.00, 46.00, 63.00, 95.00 kDa; b) Protein 230 (peak size scale): 4.50, 7.00, 15.00, 28.00, 46.00, 63.00, 95.00, 150.00, 240.00 kDa. The screening revealed the presence of compounds with a molecular weight greater than 80 kDa, in the case of Vipera aspis and Vipera xantina palestinae. For V. aspis, a 125 kDa molecular weight pro-coagulant protein was identified, known as being involved in the reduction of plasma clotting time without any direct activity in the fibrinogen coagulation process. The samples examined on the Protein 230-LabChip electrophoresis chip can be considered as a novelty with possible uses in medicine, requiring further approaches by advanced proteomics techniques to confirm the intimate structural features and biological properties of snake venoms.

由于蛇毒的生物化合物结构多样，其无疑是分子演化历程的产物：分子结构愈发复杂、特异性极高，且因潜在应用价值在医学领域极具重要性。本研究采用实用且可复现的实验方法，对9种有毒蛇类的毒液组成开展了基础性探究。本研究的目标是将该领域内蛋白质组分的检测上限拓展至230 kDa，以期实现对部分研究尚不充分的组分的鉴定。本次实验采用芯片凝胶毛细管电泳法，使用安捷伦（Agilent）2100生物分析仪搭配80与230-LabChip Protein试剂盒完成检测。电泳结果的解析采用安捷伦Protein 2100 Expert检测软件，具体参数如下：a) 蛋白80（峰尺寸标尺）：1.60、3.5、6.50、15.00、28.00、46.00、63.00、95.00 kDa；b) 蛋白230（峰尺寸标尺）：4.50、7.00、15.00、28.00、46.00、63.00、95.00、150.00、240.00 kDa。筛选结果显示，极北蝰（Vipera aspis）与巴勒斯坦蝰（Vipera xantina palestinae）的毒液中存在分子量大于80 kDa的化合物。针对极北蝰，研究人员鉴定出一种分子量为125 kDa的促凝蛋白，该蛋白可缩短血浆凝固时间，但在纤维蛋白原凝血过程中无直接活性。经Protein 230-LabChip电泳芯片检测的样本可被视为一项具有医学应用潜力的创新成果，后续需借助先进蛋白质组学技术开展进一步研究，以明确蛇毒的精细结构特征与生物学特性。