拉伸过程中粘附蛋白质复合物的解结合和解折叠：剪切和拉伸机械夹之间的相互作用
Unbinding and unfolding of adhesion protein complexes through stretching: Interplay between shear and tensile mechanical clamps
摘要：
使用粗粒度的分子动力学模拟，我们分析机械诱导的解离和展开的蛋白质复合物CD 48 - 2B 4。这种异源二聚体是免疫系统不可或缺的组成部分：2B 4是自然杀伤细胞上的受体，而CD 48在各种免疫细胞的表面上表达。到目前为止，它的机械稳定性还没有进行评估，无论是实验还是理论。我们发现，解离过程强烈依赖于方向的拉动，并可能发生在几个途径。有趣的是，CD 48 - 2B 4界面可以分为三个不同的补丁，在抵抗拉力时作为单元。在实验可达到的牵拉速度下，特征机械稳定性力在100和200 pN之间的范围内，取决于牵拉方向。这些特征力不需要与复合物分离行为中所涉及的张力相关，因为先前涉及单个蛋白质内的剪切解开可能产生更高的力峰。
英文摘要：
Using coarse-grained molecular dynamics simulations, we analyze mechanically induced dissociation and unfolding of the protein complex CD48-2B4. This heterodimer is an indispensable component of the immunological system: 2B4 is a receptor on natural killer cells whereas CD48 is expressed on surfaces of various immune cells. So far, its mechanostability has not been assessed either experimentally or theoretically. We find that the dissociation processes strongly depend on the direction of pulling and may take place in several pathways. Interestingly, the CD48-2B4 interface can be divided into three distinct patches that act as units when resisting the pulling forces. At experimentally accessible pulling speeds, the characteristic mechanostability forces are in the range between 100 and 200 pN, depending on the pulling direction. These characteristic forces need not be associated with tensile forces involved in the act of separation of the complex because prior shear-involving unraveling within individual proteins may give rise to a higher force peak.
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