New insights on growth mechanisms of protein clusters at surfaces: an AFM and simulation study
New insights on growth mechanisms of protein clusters at surfaces: an AFM and simulation study
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DOI：
10.1021/la801246k
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发表时间：
2008-09-02
期刊：
影响因子：
3.9
通讯作者：
Mulheran, P. A.
中科院分区：
文献类型：
--
作者：
Pellenc, D.;Bennett, R. A.;Mulheran, P. A.
尽管它的相关性广泛的技术和基础领域，蛋白质表面聚类动力学的定量理解往往是缺乏的。在无机晶体生长中，吸附原子的表面聚集可以用扩散-聚集模型来描述。在这类模型中，聚集体阵列的统计性质往往揭示了分子尺度的聚集过程。我们调查这些理论的潜力，揭示迄今隐藏的方面的蛋白质聚类进行伴随观察溶菌酶吸附到云母表面上，使用原子力显微镜。和Monte Carlo模拟团簇成核和生长。我们发现，溶菌酶集群扩散在基板上的速度与大小成反比。这一结果表明，哪些分子尺度的机制是负责在基板上的蛋白质的流动性。此外，还可以通过实验与模拟的比较提取单体的表面扩散系数。虽然集中在一个模型系统的溶菌酶云母，这个“概念证明”的研究成功地证明了我们的方法来理解和影响更多的生物医学适用的蛋白质底物夫妇的潜力。
Despite its relevance to a wide range of technological and fundamental areas, a quantitative understanding of protein surface clustering dynamics is often lacking. In inorganic crystal growth, surface clustering of adatoms is well described by diffusion-aggregation models. In such models, the statistical properties of the aggregate arrays often reveal the molecular scale aggregation processes. We investigate the potential of these theories to reveal hitherto hidden facets of protein clustering by carrying out concomitant observations of lysozyme adsorption onto mica surfaces, using atomic force microscopy. and Monte Carlo simulations of cluster nucleation and growth. We find that lysozyme clusters diffuse across the substrate at a rate that varies inversely with size. This result suggests which molecular scale mechanisms are responsible for the mobility of the proteins on the substrate. In addition the surface diffusion coefficient of the monomer can also be extracted from the comparison between experiments and simulations. While concentrating on a model system of lysozyme-on-mica, this 'proof of concept' study successfully demonstrates the potential of our approach to understand and influence more biomedically applicable protein-substrate couples.