Probing molecular interaction between concanavalin A and mannose ligands by means of SFM
Probing molecular interaction between concanavalin A and mannose ligands by means of SFM
复制标题
DOI：
10.1007/s00249-004-0412-5
复制
发表时间：
2004-11-01
影响因子：
2
通讯作者：
Pyka, G
中科院分区：
文献类型：
--
作者：
Lekka, M;Laidler, P;Pyka, G
近年来，扫描力显微镜（SFM）被广泛用于直接监测生物活性分子之间的特定相互作用。这些研究采用了SFM液体电池装置，它允许在自然环境中进行测量，力分辨率低至十分之一皮牛顿。本研究测定了单克隆抗人前列腺酸性磷酸酶和前列腺酸性磷酸酶的配体-受体强度，它们代表了一种具有单一类型相互作用的抗原-抗体系统。然后，测定了豆豆蛋白A与糖蛋白芳基磺化酶A和羧肽酶Y的碳水化合物组分之间的相互作用力。在人前列腺癌细胞表面寻找高甘露糖型聚糖。应用基于泊松分布的分析，在所有这些测量系统中形成的键数允许计算分子相互作用的强度。前列腺酸性磷酸酶与单克隆抗人前列腺酸性磷酸酶、刀豆蛋白A与芳基磺化酶A、刀豆蛋白A与羧肽酶Y之间的作用力分别为530+/-25、790+/-32和940+/-39 pN。根据收集的数据计算出的人前列腺癌细胞表面的魔豆蛋白A与含甘露糖配体之间的作用力值较小，为116+/-17 pN。豆豆蛋白A与含甘露糖配体之间结合力的不同值归因于碳水化合物成分的结构变化。
Recently, the scanning force microscope (SFM) has been widely used for direct monitoring of specific interactions between biologically active molecules. Such studies have employed the SFM liquid-cell setup, which allows measurements to be made in the native environment with force resolution down to a tenth of a picoNewton. In this study, the ligand-receptor strength of monoclonal anti-human prostatic acid phosphatase and prostatic acid phosphatase, representing an antigen-antibody system with a single type of interaction, was determined. Then, the interaction force occurring between concanavalin A and the carbohydrate component of the glycoproteins arylsulfatase A and carboxypeptidase Y was measured. High mannose-type glycans were sought on the human prostate carcinoma cell surface. Application of an analysis based on the Poisson distribution of the number of bonds formed in all these measured systems allowed the strength of the molecular interaction to be calculated. The values of the force acting between two single molecules were 530+/-25, 790+/-32, and 940+/-39 pN between prostatic acid phosphatase and monoclonal anti-human prostatic acid phosphatase, between concanavalin A and arylsulfatase A, and between concanavalin A and carboxypeptidase Y, respectively. The value calculated from data collected for the force between concanavalin A and mannose-containing ligands present on the surface of human prostate carcinoma cells was smaller, 116+/-17 pN. The different values of the binding force between concanavalin A and mannose-containing ligands were attributed to the structural changes of the carbohydrate components.