Institute of Applied Physics, University of Tsukuba, Tsukuba, Ibaraki, Japan.
Biopolymers. 2011 Oct;95(10):695-701. doi: 10.1002/bip.21637. Epub 2011 Apr 20.
The process of protein aggregation has attracted a great deal of research attention, as aggregates are first of all a nuisance to preparation of high quality protein and secondly used as novel materials. In the latter case, the process of protein aggregation needs to be controlled. Here, we show how arginine (Arg) regulates the process of heat-induced protein aggregation. Dynamic light scattering and transmission electron microscopy revealed that heat-induced aggregation of lysozyme at around the isoelectric point occurred in a two-step process: formation of start aggregates, followed by further growth mediated by their sticking with diffusion-limited cluster-cluster aggregation. In the presence of Arg, the diffusion-limited regime changed to reaction-limited cluster-cluster aggregation. The data indicated that the solution additives that coexisted with proteins would affect the property of the formed product, such as morphology and mechanic strength.
蛋白质聚集过程引起了广泛的研究关注，因为聚集物首先会对高质量蛋白质的制备造成干扰，其次可以作为新型材料使用。在后一种情况下，需要控制蛋白质聚集的过程。在这里，我们展示了精氨酸（Arg）如何调节热诱导蛋白质聚集的过程。动态光散射和透射电子显微镜显示，在等电点附近，溶菌酶的热诱导聚集以两步过程发生：起始聚集物的形成，然后通过其与扩散限制的簇-簇聚集的粘着进一步生长。在 Arg 的存在下，扩散限制状态转变为反应限制的簇-簇聚集。数据表明，与蛋白质共存的溶液添加剂会影响形成产物的性质，例如形态和力学强度。
