Defining the interactions between proteins and surfactants for nanoparticle surface imprinting through miniemulsion polymerization
Defining the interactions between proteins and surfactants for nanoparticle surface imprinting through miniemulsion polymerization
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DOI：
10.1021/cm702174y
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发表时间：
2008-01-08
影响因子：
8.6
通讯作者：
Tong, Yen Wah
中科院分区：
文献类型：
--
作者：
Tan, Chau Jin;Wangrangsimakul, Shalom;Tong, Yen Wah
分子印迹技术被认为是制备人工受体的最有前途的技术之一。尽管传统的印迹方法简单易行，且在小分子印迹方面取得了成功，但该方法在蛋白质大分子印迹方面存在局限性。这主要是由于与模板大分子的体积相关的有限扩散以及易碎蛋白质模板与印迹条件之间的不相容性。为了解决这些问题，成功的蛋白质印迹，细乳液聚合已被用于制备蛋白质表面印迹纳米粒子。核糖核酸酶A（RNase A），牛血清白蛋白（BSA），和溶菌酶（Lys）被用作模板蛋白质，而甲基丙烯酸甲酯和乙二醇二甲基丙烯酸酯的功能和交联单体，分别产生约40 nm的大小的颗粒。RNase A表面印迹纳米粒子在水介质中也表现出良好的分子选择性和再结合动力学。然而，这样的分子识别性能没有观察到的BSA和赖氨酸印迹纳米粒子。通过使用圆二色性研究模板蛋白-表面活性剂相互作用，发现模板蛋白和胶束之间需要一定程度的相互作用以将蛋白质保持在颗粒表面。还发现，这种相互作用不应太广泛而导致蛋白质中的显著构象变化或变性，以确保蛋白质在其天然状态下的识别。因此，本研究定义了一个简单的细乳液聚合策略，蛋白质表面印迹的成功应用所需的重要参数。
Molecular imprinting has been considered one of the most promising techniques for the preparation of synthetic receptors. In spite of the ease of the conventional imprinting methodology and its associated success with the imprinting of small molecules, the approach has its limititation for the-imprinting of protein macromolecules. This is primarily due to the limited diffusion associated with the bulkiness of the template macromolecules and the incompatibility between the fragile protein template and the imprinting conditions. To resolve these issues for the successful imprinting of proteins, miniemulsion polymerization has been employed for preparing protein surface-imprinted nanoparticles. Ribonuclease A (RNase A), bovine serum albumin (BSA), and lysozyme (Lys) were used as the template proteins while methylmethacrylate and ethylene glycol dimethacrylate were the functional and cross-linking monomers, respectively, to produce particles with sizes of about 40 nm. The RNase A surface-imprinted nanoparlicles displayed favorable molecular selectivity and rebinding kinetics even in an aqueous medium. However, such a molecular recognition property was not observed for the BSA- and Lys-imprinted nanoparticles. By studying the template protein - surfactant interaction using circular dichroism, it was found that a certain degree of interaction between the template protein and the micelles is required to maintain the proteins at the particle surface. It was also found that such an interaction should not be too extensive to cause a significant conformational change, or denaturation, in the proteins to ensure the recognition of proteins in their native states. This study therefore defines the important parameters required for the successful application of a simple miniemulsion polymerization strategy for protein-surface imprinting.