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posted by Fnord666 on Thursday October 31 2019, @12:14PM   Printer-friendly
from the sometimes-disordered-is-good dept.

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.

In their recent paper, Ashutosh Chilkoti, the chair of Duke Biomedical Engineering, and Felipe Garcia Quiroz, a Ph.D. graduate of the Chilkoti Lab who is a postdoctoral fellow at Rockefeller University, demonstrate that they can precisely tune the stability of IDP-based materials by controlling how quickly IDPs associate and dissociate in response to environmental cues.

"Unlike well-folded proteins, conventional IDPs have a hard time shielding different parts of their structures from each other," Quiroz said. "So as IDPs become more abundant in a solution they begin to collide and clash frequently, with some of their exposed structures weakly sticking together and rapidly breaking apart."

[...] Because current IDP-based materials lack stability, their effect is short-lived as they erode fairly quickly, but this new approach could make IDPs a good source of new materials for wound-healing.

"IDPs have had a set of known characteristics, and we have been working within that range of characteristics to explore potential biomedical applications for the last two decades," Quiroz said. "But now we essentially have new tools to play with, and that allows us to be more creative. Our discovery adds complexity to what we are able to do with IDP-based materials for applications spanning materials science and biology, which is exciting."

More information: Felipe Garcia Quiroz et al. Intrinsically disordered proteins access a range of hysteretic phase separation behaviors, Science Advances (2019). DOI: 10.1126/sciadv.aax5177


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  • (Score: 2) by HiThere on Thursday October 31 2019, @03:53PM (1 child)

    by HiThere (866) Subscriber Badge on Thursday October 31 2019, @03:53PM (#914184) Journal

    The things that normally shape the proteins are called prions. Usually they're only noticed when they get out of whack and cause something like scrapie or mad cow disease. So I'd be a bit careful about using this for wound healing.

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  • (Score: 0) by Anonymous Coward on Thursday October 31 2019, @06:47PM

    by Anonymous Coward on Thursday October 31 2019, @06:47PM (#914278)

    Proteins are shaped by how certain amino acids within the protein interact (ie: bond) with other amino acids within the protein and by what other proteins/particles/chemicals exist in their environment and how those proteins interact with the environment. Factors such as pH and temperature may also affect shape.