Technion solves decades-old problem surrounding protein synthesis

Until now, scientists had no choice but to allow proteins to fold in whichever way it falls, with the process taking hours to days with expected loss in material along the way.

A model of the protein (the blue ribbon) and the DNA (the spheres) is binds (photo credit: WEIZMANN INSTITUTE OF SCIENCE)
A model of the protein (the blue ribbon) and the DNA (the spheres) is binds
(photo credit: WEIZMANN INSTITUTE OF SCIENCE)
Researchers at the Technion - Israel Institute of Technology made an important series of breakthroughs within protein synthesis that potentially hold major medical implications.
The researchers had five articles accepted for publication in scientific research journals, each publication will deal with a novel method of protein synthesis, and its implementation in the development of pharmacologically important molecules.
“We anticipate the new synthesis strategies will be a gamechanger in developing new drugs for cancer, intestinal diseases, diabetes, and more,” said Technion Prof. Ashraf Brik of the Schulich Faculty of Chemistry.
Proteins, which are chained together amino acids folded onto itself, are difficult to create artificially. Scientists are able to recreate the chain, but to have it fold onto itself is another challenge that has escaped researchers for decades.
"One element of this challenge is a particular amino acid, cysteine, which forms a disulphide bond with another cysteine along the chain," the Technion explained in a statement. "If there is only one other cysteine on the chain, the bond will be formed, and the protein will fold the way it should."
Until now, scientists had no choice but to allow proteins to fold in whichever way it falls, with the process taking hours to days with expected loss in material along the way.
The Technion research bypasses that and found two molecular “cages” that protect proteins with two individual cysteines.
"One ‘cage’ is unlocked by palladium, and the other by exposure to UV light," the university explained. "When they are unlocked in sequence, only two cysteines are exposed simultaneously, thus only the correct disulphide bond can be formed."
Using the method, the team successfully synthesized "correctly folded peptides and proteins with up to three disulphide bonds in less than 15 minutes, in one container, and without much material loss."