心臟毒素蛋白在眼鏡蛇蛇毒中佔了約二分之一的量，但其對動物的毒性約只有蛇毒素中神經毒素的十分之一。這個60至62胺基酸，以□摺板為主的鹼性蛋白，以演化的觀點來說，如此多的量卻又不是眼鏡蛇毒殺生物的主要分子，想必有其其他功能才是。但是從1947年發現至目前為止，除了不算強的毒殺細胞能力外，尚未找出其他具專一性的功能，即使是毒殺細胞一事，其毒殺之分子機制也尚無確切的了解。由過去的研究發現，心臟毒素與負電荷的脂質膜有很強的結合能力，也會造成細胞膜的導電性增加，因此目前大多數認可的生物作用機制是心臟毒素作用於細胞膜上的脂質分子並擾動了膜的通透性而造成了細胞的死亡。
在此論文中利用各種光譜技術及電腦模擬方法嘗試將心臟毒素作用於人工細胞膜上的過程一一分析釐清，其所獲得的結論有下列幾點。

一、 當心臟毒素結合於負電脂質膜時，除了結合強度上比中性脂質強之外，其結合的模式也不一樣。在負電脂質膜上，心臟毒素會聚集成多聚體並形成直徑2.5~10奈米之孔洞，造成細胞膜的洩漏。

二、 以單層分子膜技術使心臟毒素與脂質膜的結合被固定在初始結合步驟時可以發現，在中性與負電性脂質上的結合方式大致相同，心臟毒素以48度斜角插於膜上，插入深度則是負電性脂質膜較深。以平均埸方法計算心臟毒素結合於膜上之模式發現改變脂質膜頭部電位可以使心臟毒素由表面結合模式轉變為深埋插入模式。

三、 水溶液中的心臟毒素結合到負電性脂質膜後會進行一連串的後續過程，從單體聚集成多聚體(幾秒)、形成孔洞(幾十秒)、孔洞閉合(十幾毫秒)、形成非孔洞之抗水解酵素複合體(約一分鐘)。

雖然心臟毒素與人工脂質膜的交互作用研究目前已有稍具清晰的梗概，但對其在真實世界中所扮演的角色仍是曖昧不清。如果要說此篇論文對心臟毒素在生物上的作用有了更多的了解，我並不敢如此地說，比較合適的說法是透過心臟毒素與負電性脂質膜的研究讓我們對膜活性分子與細胞膜的作用有了較多的認識。心臟毒素與生物細胞的作用機制的了解我想需要更多研究者的投入及更大的想像力之挹注。

The Study of Pore Formation Mechanism of the Cobra Cardiotoxin on Membranes.

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