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The initial proof of this concept demonstrates the potential for this process to enhance the detection abilities of many currently employed immunosensor technologies
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Description: A method for covalently attaching peptides and small molecules to antibodies through a highly conserved binding domain located on the antibody Fab fragment. This conserved domain has been observed across all species and all immunoglobulin isotypes an provides for an excellent insertion location for near limitless possible functional moieties. Through an in silico screening of small molecules and experimental verification we were able to select for a small molecule that selectively binds to this conserved binding domain. Once associated, a stable covalent bond is formed through a photo-chemical reaction in a UV energy dependent manner. This results in a unique and consistent covalent insertion of a target molecule selectively to the antibody light chains that does not disrupt the antibodies ability to bind its respective antigen nor impact Fc recognition. Using this method we have been able to develop a immunosensor that maintains nearly 100% antibody activity through the oriented immobilization of antibodies onto an ELISA surface. Current immunosensors often rely on the random orientation of antibodies nonspecifically adsorbed to the surfaces which renders up to 90% of antibodies inactive through sterically hindering access to their binding sites or egatively impacting antibody conformation. Validation of this initial proof of concept demonstrates the potential for this process to enhance the detection abilities of many currently employed immunosensor technologies as well as detection modalities currently being developed for lab-on-a-chip application. This method of crosslinking also has implications in the development of next generation pharmaceutical antibodies by providing a site specific insertion of function moieties (without disrupting natural antibody immune activation) such as: chemotherapeutics, cell penetrating peptides, targeting sequences, imaging specific molecules, and facilitates oriented immobilization of antibodies onto a number of nanoparticle drug delivery platforms (such as liposomes).