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Argonne Researchers Develop Method that Aims to Stabilize Antibodies
Date:9/3/2009

. These chains are made up of modules known as constant and variable domains. The light and heavy chain each has a variable domain, which come together to form the antigen binding site. Because of the great diversity of amino acids in the variable domains, different antibodies are capable of interacting with an effectively unlimited number of targets.

Sometimes this variability comes at a price; the amyloid-forming light chains were less stable than their normal counterparts. However, even amyloid-forming light chains have amino acid substitutions that improve stability. When seven of these amino acid changes were introduced into an amyloid-forming variable domain, a billion-fold improvement in thermodynamic stability was obtained reflecting a much higher ratio of native protein folds to unfolded proteins - a major determinate of antibody shelf life.

"Our work at this detailed level has taught us that antibody stabilization was possible, but we needed to find out if antibodies could be stabilized without compromising their function and do so with moderate experimental investment," Stevens said. Recent work suggests these goals are potentially achievable. To proactively improve the stability of a different antibody variable domain, Argonne researchers drew up a short list of 11 candidate amino acid changes. Four of the amino acid changes improved antibody stability and when combined together in the original domain provided a 2,000-fold improvement in stability.

A follow up experiment using a functional antibody fragment was able to improve antibody stability comparably, with no loss of antibody functionality. Both experiments required approximately one month to accomplish instead of the potentially open-ended time required for most protein stabilization projects.

There is a correlation between thermodynamic stability and thermal stability, the billion fold improvement in thermodynamic stability increased the therm
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