Tech.Sight. Antibody design by man and nature.
Catalytic antibodies have emerged as being without peer as rationally designed biocatalysts. They have been shown to catalyze an ever-increasing array of chemical reactions with both high substrate specificity and selectivity. Probing the immune repertoire, via an expanding number of techniques, has lead to the production of proteins that can catalyze chemistry that is both difficult to perform using existing chemical methods and that is not catalyzed by endogenous enzymes. Remarkably, recent evidence has pointed to a hitherto unknown catalytic function of all antibodies that seems to be intrinsic to their immunoglobulin structure, the conversion of 1O2* into H2O2. This new catalytic potential of antibodies points to a new 'chemical arm' of the immune system and reveals that the evolution of catalytic antibodies significantly predates their rational design.
Wentworth
Paul
P
Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. paulw@scripps.edu
D000818:Animals; D017151:Antibodies, Catalytic / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D000911:Antibodies, Monoclonal; D002384:Catalysis; D003001:Cloning, Molecular; D006241:Haptens / Q000276:immunology; D006801:Humans; D006825:Hybridomas; D006861:Hydrogen Peroxide / Q000378:metabolism*; D007114:Immunization; D051379:Mice; D019151:Peptide Library; D026082:Singlet Oxygen / Q000378:metabolism*; D013379:Substrate Specificity
D017151:Antibodies, Catalytic; D000911:Antibodies, Monoclonal; D006241:Haptens; D019151:Peptide Library; D026082:Singlet Oxygen; D006861:Hydrogen Peroxide