How Stabilizing Disordered Proteins May Lead To The Next Generation Of Medical Applications

Arthur T Knackerbracket writes:

Arthur T Knackerbracket has found the following story:

Biomedical engineers from Duke University have demonstrated that they can create stable materials from engineered disordered proteins by altering the environmental triggers that cause them to undergo phase transitions.

This discovery shines a light on previously unexplored behaviors of disordered proteins and allows researchers to create novel materials for applications in drug delivery, tissue engineering, regenerative medicine and biotechnology.

The research appeared online on Oct. 18 in Science Advances.

Proteins function by folding into 3-D shapes that interact with different biomolecular structures. Researchers previously believed that proteins needed to fold into a specific fixed shape in order to function, but in the last two decades, engineers seeking to create novel materials for biomedical applications have turned their attention to intrinsically disordered proteins, called IDPs, which dynamically shift among a wide array of structures.

IDPs are especially useful for biomedical purposes because they can undergo phase transitions -- changing from a liquid to a gel, for example, or a soluble to an insoluble state, and back again -- in response to environmental triggers, like changes in temperature. This ability has made IDPs a go-to tool for long-term drug delivery, as IDPs can be injected in liquid form into the body and then solidify into a gel depot that slowly releases medication.

But while their flexible structure makes IDPs useful in a variety of applications, researchers previously thought that this flexibility limited the stability of the resulting materials.

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