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Science 14 February 1997:
Vol. 275. no. 5302, pp. 945 - 948
DOI: 10.1126/science.275.5302.945
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Research Articles

Chemical Selection for Catalysis in Combinatorial Antibody Libraries

Kim D. Janda, * Lee-Chiang Lo, Chih-Hung L. Lo, Mui-Mui Sim, Ruo Wang, Chi-Huey Wong, * Richard A. Lerner *

For the past decade the immune system has been exploited as a rich source of de novo catalysts. Catalytic antibodies have been shown to have chemoselectivity, enantioselectivity, large rate accelerations, and even an ability to reroute chemical reactions. In many instances catalysts have been made for reactions for which there are no known natural or man-made enzymes. Yet, the full power of this combinatorial system can only be exploited if there was a system that allows for the direct selection of a particular function. A method that allows for the direct chemical selection for catalysis from antibody libraries was so devised, whereby the positive aspects of hybridoma technology were preserved and re-formatted in the filamentous phage system to allow direct selection of catalysis. This methodology is based on a purely chemical selection process, making it more general than biologically based selection systems because it is not limited to reaction products that perturb cellular machinery.

The authors are at The Scripps Research Institute, Department of Chemistry and the Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
*   To whom correspondence should be addressed.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Phage display of a catalytic antibody to optimize affinity for transition-state analog binding.
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X-ray structures of a hydrolytic antibody and of complexes elucidate catalytic pathway from substrate binding and transition state stabilization through water attack and product release.
B. Gigant, J.-B. Charbonnier, Z. Eshhar, B. S. Green, and M. Knossow (1997)
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