Temperature-responsive protein pores
Temperature-responsive protein pores
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DOI：
10.1021/ja065827t
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发表时间：
2006-11-29
影响因子：
15
通讯作者：
Movileanu, Liviu
中科院分区：
文献类型：
--
作者：
Jung, Yuni;Bayley, Hagan;Movileanu, Liviu
我们描述了含有单个弹性蛋白样多肽（ELP）环的温度响应性蛋白孔。将ELP环置于α-溶血素（α HL）孔（一种已知晶体结构的七聚体）的内腔腔内。空腔大致为球形，分子表面体积约为39500埃（3）。在施加的电位下，野生型α HL孔长时间保持开放。与此相反，ELP环含有α HL孔表现出瞬态电流阻断，其性质取决于插入的环的长度和序列。与聚（乙二醇）共价连接的空腔内获得类似的结果一起，数据表明，瞬态电流封锁是由ELP到跨膜SS-桶域的孔的偏移所造成的。低于其转变温度，ELP环完全膨胀并完全但可逆地阻塞孔。在其转变温度以上，ELP脱水，结构坍塌，使大量的离子流动。讨论了温度响应性蛋白质孔在医学生物技术中的潜在应用。
We describe temperature-responsive protein pores containing single elastin-like polypeptide (ELP) loops. The ELP loops were placed within the cavity of the lumen of the alpha-hemolysin (alpha HL) pore, a heptamer of known crystal structure. The cavity is roughly spherical with a molecular surface volume of about 39 500 angstrom(3). In an applied potential, the wild-type alpha HL pore remained open for long periods. In contrast, the ELP loop-containing alpha HL pores exhibited transient current blockades, the nature of which depended on the length and sequence of the inserted loop. Together with similar results obtained with poly(ethylene glycols) covalently attached within the cavity, the data suggest that the transient current blockades are caused by excursions of ELP into the transmembrane ss-barrel domain of the pore. Below its transition temperature, the ELP loop is fully expanded and blocks the pore completely, but reversibly. Above its transition temperature, the ELP is dehydrated and the structure collapses, enabling a substantial flow of ions. Potential applications of temperature-responsive protein pores in medical biotechnology are discussed.