Multivalent Antibody Aggregation
by young on Feb.07, 2010, under ChemSem 03, _Spring 2010
On January 28, 2010, Basar Bilgicer who is a professor at University of Notre Dame visited Andrews University for his presentation. Mr. Basar Bilgicer prepared two presentations. One of them was “Peptide Design Using Unnatural Amino Acids.” The other was “Multivalent Antibody Aggregation.” More students in the presentation wanted to know about the antibody aggregation. Therefore, he started the presentation, introducing us the basis of antibody. Especially, he talked about IgG antigen. Overall, he showed us a lot of illustrations which explained how the antibody which has bivalency or trivalency worked with antigens and ligands. Also, he used chromatographic graphs which supported his experimental results. It made me easy to understand how the antibody aggregates in various ways.
There were several kinds of ways which antibody binds to antigen or ligands. Largely, the antigens were divided up depending on the shape, whether they are bivalent, or trivalent. Then, they generated several aggregates, such as dimer, trimer, tetramer, or polymer. They also were produced in a cyclic form, a linear form, or in the middle.
During the presentation, he gave details about the correlation between the Gibbs free energy and the binding constant. I asked him about the effects of temperature on the binding constant. He answered that denaturing occurs above five to ten Celsius degree than the body temperature and the binding constant decreases as the temperature decreases under room temperature.
I would tell my friends that the presentation was about the kind of how and what is involved in binding between antibodies and antigens, or ligands.
Tell A Friend
