The interplay between binding energy and catalysis in the evolution of a catalytic antibody

Article Abstract:

Researchers studied the development of binding energy and its relation to catalytic function in the evolution of the catalytic antibody AZ-28. They reconstructed the pure germline with no somatic mutations, and introduced the six somatic mutations individually and in combinations. This causes a small increase in binding affinity, which affects the alignment of diene and phenyl orbitals, resulting in a decrease in rate. The combinatorial diversity of the immune system provided an efficient antibody catalyst for the oxy-Cope rearrangement of AZ-28, for which there is no known enzyme, and the opportunity to study the process of biological catalysis.

Catalysis, Binding energy

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Transition-state stabilization as a measure of the efficiency of antibody catalysis

Article Abstract:

There are 60 known reactions which are successfully catalyzed by monoclonal antibodies, which have been observed to also catalyze reaction pathways that are normally not favored kinetically. Transition-state theory was used to conduct a quantitative analysis of the scope and limits of antibody catalysis. The results showed that the ratio of equilibrium-binding constants of the reaction substrate and the transition-state analog used to raise the antibody may be used to predict the observed reaction rate accelerations.

Chemical reaction, Rate of, Chemical kinetics

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