A team of biochemists at the University of Washington has developed a means for engineering proteins that can transition between assembly and disassembly via allosteric control. In their paper published in the journal Nature, the group details their engineering process and how well it has worked thus far during testing.
A. Joshua Wand, with Texas A&M University, has published a News and Views piece in the same journal issue explaining why being able to get a protein to assemble or disassemble in the presence of an effector has been an important goal of chemists and outlines the work done by the team on this new effort.
Prior research has shown that if chemists could build proteins that assemble themselves into desired shapes on command, the results could be used for highly specific purposes, such as building a cage-shaped protein to carry a drug to a certain part of the body for therapeutic purposes.
Prior research has also shown that if such a mechanism could be developed, via a process known as allosteric regulation, a specific trigger would be needed—one that chemists refer to as an effector. To achieve this feat, the research team used several techniques they previously developed.
One such technique involved using an AI app to help predict a protein structure given a list of attributes. Another involved creating a protein with a hinge that was able to take on two different forms. And a third involved a way to connect certain proteins together.
By Bob Yirka
Article can be accessed on: phys.org