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Molecules 2003, 8(1), 86-91; doi:10.3390/80100086

Atomic Force Microscope Imaging of the Aggregation of Mouse Immunoglobulin G Molecules

Department of Chemistry, Jinan University, Guangzhou, 510632, China
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Author to whom correspondence should be addressed.
Received: 1 January 2003 / Published: 31 January 2003
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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 Mouse immunoglobulin G; self-assembly; aggregation; atomic force microscope
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

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.

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