Manipulation of Proteins on Mica by Atomic Force Microscopy.
Manipulation of Proteins on Mica by Atomic Force Microscopy.
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DOI：
10.1021/la00037a015
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发表时间：
1992
期刊：
影响因子：
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通讯作者：
A. Lea;A. Pungor;V. Hlady;J. Andrade;J. Herron;E. Voss
中科院分区：
文献类型：
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作者：
A. Lea;A. Pungor;V. Hlady;J. Andrade;J. Herron;E. Voss
利用原子力显微镜实时成像了单抗IgM在云母上的吸附情况。在我们所能达到的最小力(~lt；4nN)下，悬臂尖端表现为分子扫帚的行为，并被观察到以垂直于悬臂尖端小面的方向排列的链状蛋白质聚集体。旋转扫描方向保持了方向关系，如旋转的链的形成所示。当施加的力增加时，链之间的距离增加，这表明可以扫描的蛋白质的量取决于施加的力。扫描效果增加了IgM表面的表观覆盖率。仅在数十分钟后才观察到具有4-NN排斥力的沉积的纤维蛋白原层的操纵，但还没有达到形成链的程度，这表明纤维蛋白原与云母之间的粘附力大于IgM与云母之间的粘附力。在30nN的排斥力下，纤维蛋白原链形成，蛋白质被操纵产生大写字母U。在更高的排斥力下，整个扫描区域被扫得干干净净。
The atomic force microscope was used to image adsorption of a monoclonal IgM on mica in real time. Under the smallest possible force we could achieve (<4 nN), the cantilever tip behaved as a molecular broom and was observed to orient protein aggregates in strands oriented perpendicularly to the facet of the cantilever tip. Rotating the scan direction preserved the orientational relationship, as seen by the formation of rotated strands. When the applied force was increased, the distance between the strands increased, indicating the amount of protein that can be swept depends on the applied force. The effect of scanning increased the apparent surface coverage of IgM. Manipulation of a deposited fibrinogen layer with a 4-nN repulsive force was observed only after tens of minutes, but not to the extent that strands formed, indicating a greater adhesion between the fibrinogen and mica than between IgM and mica. With an applied repulsive force of 30 nN, fibrinogen strands formed and the protein was manipulated to produce the block letter U. At a much higher repulsive force, the entire scanning area was swept clean.