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Animal venoms are intricate and teem with potential for groundbreaking medical advancements. Although traditional methods for purifying venom proteins are effective, they usually require complicated, multi-step processes that lead to lower yields. Our study introduces an efficient, one-step technique for extracting venom-derived proteins through reverse-phase high-performance liquid chromatography (RP-HPLC). We carefully optimized the RP-HPLC process, focusing on the gradient elution conditions and the strategic use of our columns’ stationary phase characteristics, to enhance the effectiveness of our separations. This enabled us to efficiently isolate six venom proteins: melittin (2.846 kDa) from <i>Apis mellifera</i> with a yield of 4.5% and homogeneity of 99%; α-cobratoxin (7.821 kDa) from <i>Naja kaouthia</i> with a yield of 15% and homogeneity of 99%; α-bungarotoxin (7.983 kDa) from <i>Bungarus multicinctus</i> with a yield of 7% and purity of 99%; calciseptine (7.035 kDa) from <i>Dendroaspis polylepis</i> with a yield of 6% and homogeneity of 95%; notexin (13.593 kDa) from <i>Notechis scutatus</i> with a yield of 10% and homogeneity of 95%; and CVFm (150 kDa) from <i>Naja melanoleuca</i> with a yield of 0.8% and homogeneity of 94%. These were all accomplished in one step. This breakthrough simplifies the purification of venom peptides and proteins, making the process more feasible and economical. It paves the way for developing new drugs and promising treatments that are both more effective and precisely targeted.