In a new paper in Biomacromolecules, researchers from Nicholas Peppas’ Laboratory of Biomaterials, Drug Delivery, and Bionanotechnology describe unexpected results in the field of protein imprinting.
Graduate student Heidi Culver originally set out to develop protein-imprinted polymers with a biodegradable core, which are synthetic materials engineered to have molecular recognition properties, similar to an antibody or an enzyme. These polymers, which mimic enzymes and antibodies, could be used in many applications such as drug delivery, clearing of toxic materials from the body, and imaging, among others. These synthetic polymers can be produced at a lower cost with more environmental stability than an enzyme or an antibody.
Researchers also made an important finding about protein imprinting itself. It has been widely believed that imprinted proteins lead to selectivity of protein binding, but graduate student Heidi Culver has found that it is actually the formulation of the polymer itself, which leads to protein binding, rather than the imprinting process.
This is important because it’s a change in the original theory about the cause of protein binding. Culver’s research provides a fundamental analysis on the architecture of molecular materials used to deliver drugs, which will lead to a more informed understanding in the field of imprinted polymers.
Read more at Biomacromolecules.
