Immobilization of enzyme on chiral polyelectrolyte surface

Chiral D- and L-N-acryloyl aspartic acid (NAsp) polyelectrolyte (PE) surfaces with similar chemical compositions and physical properties but opposite chirality are designed for enzyme immobilization . Enzymes immobilized onto the chiral PE surfaces present high chiral preference, namely L-NAsp PE surface can keep most of the catalytic activity of the immobilized enzymes , however, for enzymes immobilized on D-NAsp PE surface a large decrease in catalytic activity occurred which was 11 times lower compared with L-NAsp PE surface. This phenomenon of chiral effect on enzymes immobilization can be explained by attenuated total reflectance (ATR) and circular dichroism (CD) results. The results exhibited that L-NAsp PE surface could preserve most of the secondary structures of immobilized enzymes while on D-NAsp PE surface with a large conformation alteration. These chiral surface induced differences after enzyme immobilization can be further used for logic operation. These results imply a novel strategy for the design of new enzymes immobilization materials based on the chiral effect and expand the applications of enzymes in biochips , chemical transformations and chiral biodevices.