BACKGROUND
Proteins are incredibly useful in medicine and industrial chemistry. Many of the most recent breakthroughs in cancer therapy are based on monoclonal antibody treatments. Yet, there are major difficulties that can act as deterrents in developments of such therapies. Similarly, usage of proteins as enzymes is limited by poor stability, short half-life, and difficulties with reusability. With growing usage of proteins as pharmaceuticals and biocatalysts, and apparent shortcomings in both fields, there is a growing need to design materials that are protein compatible and can improve protein stability.
SUMMARY OF TECHNOLOGY
Here a biomimetic strategy inspired by several living organisms is used to maintain protein (enzyme or therapeutic) function by a network of superhydrophilic and osmolyte polymers. Here, zwitterionic microscale hydrogels of two different zwitterionic moieties (carboxybetaine and sulfobetaine), were synthesized, using an inverse emulsion, free radical polymerization reaction technique. Microscale hydrogels were loaded with proteins using a post-fabrication loading technique which prevents unwanted reactions. Protein loading and released from these hydrogels were studied to develop the polymeric network which can increase the protein stability for therapeutic purposes. Furthermore, a reaction scheme was developed and studied for covalent immobilization of protein within the zwitterionic microscale hydrogels. The enzymatic activity of proteins loaded/released, or proteins immobilized within zwitterionic hydrogels were studied. Our result show increased the conformational stability and half-life of the proteins by using microscale zwitterionic hydrogels. This technology has direct applications for subcutaneous delivery of biologics as well as fabrication of enzyme immobilized materials with extend enzyme lifetime and molecular turnover.
POTENTIAL AREAS OF APPLICATION
MAIN ADVANTAGES
STAGE OF DEVELOPMENT