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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Single molecular dynamic interactions between glycophorin A and lectin as probed by atomic force microscopy.
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Single molecular dynamic interactions between glycophorin A and lectin as probed by atomic force microscopy.

机译：原子力显微镜探测的血型糖蛋白A和凝集素之间的单分子动力学相互作用。

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摘要

Glycophorin A (GpA) is one of the most abundant transmembrane proteins in human erythrocytes and its interaction with lectins has been studied as model systems for erythrocyte related biological processes. We performed a force measurement study using the force mode of atomic force microscopy (AFM) to investigate the single molecular level biophysical mechanisms involved in GpA-lectin interactions. GpA was mounted on a mica surface or natively presented on the erythrocyte membrane and probed with an AFM tip coated with the monomeric but multivalent Psathyrella velutina lectin (PVL) through covalent crosslinkers. A dynamic force spectroscopy study revealed similar interaction properties in both cases, with the unbinding force centering around 60 pN with a weak loading rate dependence. Hence we identified the presence of one energy barrier in the unbinding process. Force profile analysis showed that more than 70% of GpAs are free of cytoskeletal associations in agreement with previous reports.
机译：糖皮质激素A（GpA）是人类红细胞中最丰富的跨膜蛋白之一，其与凝集素的相互作用已作为与红细胞相关的生物学过程的模型系统进行了研究。我们使用原子力显微镜（AFM）的力模式进行了力测量研究，以研究参与GpA-凝集素相互作用的单分子水平生物物理机制。将GpA固定在云母表面或天然存在于红细胞膜上，并通过AFM探针进行探针探测，该探针通过共价交联剂涂有单体但多价的维氏假单胞菌凝集素（PVL）。动态力谱研究表明，在两种情况下相互作用特性相似，解开力集中在60 pN左右，且加载速率依赖性较弱。因此，我们确定了解除绑定过程中存在一个能量屏障。力谱分析表明，与以前的报道一致，超过70％的GpA没有细胞骨架结合。

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