Peptide Design Using Unnatural Amino Acids and Multivalent Antibody Aggregation by Basar Bilgicer
by seonui on Feb.07, 2010, under ChemSem 03, _Spring 2010
The guest speaker of the chemistry seminar held on January 28 was Basar Bilgicer, who is an assistant professor in the Department of Chemical & Biomolecular Engineering at University of Notre Dame. During the presentation, he focused on antibodies, such as IgG, and their aggregations to form multivalent molecules in biological systems and friendly explained about them. I think his seminar really helped students get a deeper understanding of antibody aggregation.
I was very interested in the pathway to make cyclic dimers and trimers from monomers. Bivalent hapten makes it possible to generate several forms of aggregations such as trimer, tetramer, and other polymers. Moreover, depending on the concentration of the ligands that bind to the tips of antibody, more complex form can be produced. For example, a synthetic trivalent hapten, which is monocyclic, aggregates IgG into bicyclic trimers. Through his presentation, I also learned about the thermodynamics and kinetics of multivalent molecules of antibodies, based on the basic dynamic principles. For example, the bicyclic trimer is kinetically and thermodynamically more stable than monomeric aggregates of this IgG.
On the other hand, I have a question about the aggregation of other antibodies rather than IgG antibody that he focused on for his research and about the potential application of antibody aggregates in future biotechnology.
I would say to my ‘non-science’ friends or family that the study of antibody is very important for design of diagnostic molecules for therapy of diseases, and Dr. Bilgicer has worked in multivalent interactions of antibody aggregation in biological systems.
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