Enzyme-Stabilizing Hydrogels

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Background: Immobilization of biomolecules (i.e. proteins, enzymes) has significant implications in energy production, pharmaceutical synthesis, and drug screening. More recently, interfacial thin-film hydrogels enabling the stable encapsulation of enzymes have attracted interest in the biosensing field due to their potential to be incorporated into high throughput screening (HTS)screens in which high numbers of small volume samples can be tested.Traditional HTS methods present various challenges including false-positive hits and non-specific and/or promiscuous behaviour of compounds, typically due to aggregates that physically block (rather than biochemically bind to) an enzyme active site. As a result, time and money are lost chasing false lead compounds. To-date, there has been limited success in the discovery of methods to quickly identify these promiscuous compounds and aggregates. Technology Overview To address this, McMaster researchers have developed a printable hydrogel based drug-screening platform that can immobilize a bioactive biomolecule and control access to that biomolecule based on the hydrogel pore size. This approach is highly beneficial in drug discovery and early stage pharmaceutical testing and analysis because it provides the ability to discriminate between true enzyme inhibitors and promiscuous inhibitors for lead enzyme-targeting drugs while significantly reducing (by up to 95%) the amount of sample required for screening. This saves time and money when conducting HTS while resulting in significantly fewer false-positive hits. The hydrogel is also printable using an ink jet printer without requiring external activation. Stage of Development: Proof of principle data is available. Publication: https://www.nature.com/articles/s41467-018-02956-z 17-072