Abstract: Mouse immunoglobulin G (Ig G1 and the mixture of Ig G1 and Ig G2) deposited on mica were imaged with an atomic force microscope at room temperature and ambient pressure. At a concentration around 1.0mg/L, the molecules were well dispersed. 2~3 days after sample preparation, both Ig G1 and the mixture could self- assemble into different shapes and further form some types of local-ordered toroidal aggregations (monotoroidal, intercrossed toroidal, concentric toroidal, etc.). The number of monomers was not identical in the different toroidal aggregations but in a same circle, the shapes of polymer self-assembled by several monomolecules were found to be almost the same. There was difference between the aggregation behavior of Ig G1 and the mixture. The mechanism of Ig G molecule aggregation was ascribed to the “Y” shape and loops structure of Ig G molecule.
Keywords: Mouse immunoglobulin G; self-assembly; aggregation; atomic force microscope
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Cai, J.; Chen, Y.; Xu, Q.; Chen, Y.; Zhao, T.; Wang, X.; Xia, K. Atomic Force Microscope Imaging of the Aggregation of Mouse Immunoglobulin G Molecules. Molecules 2003, 8, 86-91.
Cai J, Chen Y, Xu Q, Chen Y, Zhao T, Wang X, Xia K. Atomic Force Microscope Imaging of the Aggregation of Mouse Immunoglobulin G Molecules. Molecules. 2003; 8(1):86-91.
Cai, Jiye; Chen, Yao; Xu, Qingcai; Chen, Yong; Zhao, Tao; Wang, Xiaoyan; Xia, Ke. 2003. "Atomic Force Microscope Imaging of the Aggregation of Mouse Immunoglobulin G Molecules." Molecules 8, no. 1: 86-91.