Reversible "irreversible" inhibition of chymotrypsin using nanoparticle receptors
Reversible "irreversible" inhibition of chymotrypsin using nanoparticle receptors
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DOI：
10.1021/ja0352505
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发表时间：
2003-11-05
影响因子：
15
通讯作者：
Rotello, VM
中科院分区：
文献类型：
--
作者：
Fischer, NO;Verma, A;Rotello, VM
阴离子功能化的两亲性纳米粒子通过静电结合随后蛋白质变性有效地抑制胰凝乳蛋白酶。我们证明了通过使用阳离子表面活性剂修饰纳米颗粒表面来破坏这种“不可逆”的胰凝乳蛋白酶抑制的能力。在添加长链表面活性剂后，可挽救高达50%的原始胰凝乳蛋白酶活性。动态光散射研究表明，糜蛋白酶从纳米颗粒表面释放。救援糜蛋白酶的构象，其特征在于通过荧光和荧光各向异性，表明糜蛋白酶恢复了高度的天然结构后，表面活性剂添加。
Anionically functionalized amphiphilic nanoparticles efficiently inhibit chymotrypsin through electrostatic binding followed by protein denaturation. We demonstrate the ability to disrupt this "irreversible" inhibition of chymotrypsin through modification of the nanoparticle surface using cationic surfactants. Up to 50% of original chymotrypsin activity is rescued upon long-chain surfactant addition. Dynamic light-scattering studies demonstrate that chymotrypsin is released from the nanoparticle surface. The conformation of the rescued chymotrypsin was characterized by fluorescence and fluorescence anisotropy, indicating that chymotrypsin regains a high degree of native structure upon surfactant addition.