CHEM564 Lecture Notes - Lecture 1: Hydrazine, Aldehyde, Ethanolamine
2 May 2017
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Document Summary
Protein immobilization chemistry generally takes advantage of amine or carboxylate functional groups on proteins. A problem with this approach in solution is that the proteins themselves have multiple copies of each functional group (except in rare instances). Thus, in solution, addition of a coupling agent (such as edci) will result in a complex mixture of crosslinked proteins unless carefully controlled (scheme i). By moving one of the components to a surface, we can easily control the relative concentrations of the functional groups, and prevent undesired interactions. An excellent illustration of protein crosslinking chemistry can be found in the use of surface plasmon resonance (spr). Spr can be used to detect the binding of biomolecules to a surface in real time, and therefore provides a window to thermodynamic and kinetic features of these interactions. The simplest form of an spr experiment would be to immobilize an antibody to the surface, and detect the binding of a protein antigen.
