Researchers at the Biodesign Institute's Center for Innovations in Medicine at Arizona State University have introduced a groundbreaking process for creating antibodies by manufacturing synthetic antibodies, called synbodies. The research is published in the current issue of PLos ONE.

"We turned the process on its head," said Stephen Johnston, researcher and director of the Center for Innovations in Medicine at ASU. "If you design these chemical antibodies right, they should have a high probability of binding to something."

The researchers developed a technique to construct amino acid sequences and link them together, forming a synbody. These synbodies can bind with at least one of the tens of thousands of human proteins, called the proteome, according to the report.

In order to work backward, Johnston, researcher Chris Diehnelt and their team joined together 20-unit random sequences of amino acids, forming peptides. Uniting two of these peptides chemically creates a ligand, or bonding agent, Johnston explained to DOTmed News. This ligand can attach to a specific protein, working as a synthetic antibody.

"Most antibodies work by a lock-and-key mechanism," said Johnston. "You hold something very rigid and figure out what part of the target it could bind to...We did it differently than nature does it to make it simpler."

Instead of presenting a protein to an antigen- the target - to create an antibody, Johnston's method creates an antibody and then uses its "floppy-armed" structure to try to find what it could bind to, out of thousands of proteins on an array slide. The arms literally flail around and grab onto proteins, he said.

The only disadvantage, explained Johnston, is that the researchers can't predict which of the some 20 thousand proteins, if any, the synbody will bind to. Johnston relates the process to the lottery.

In this particular research, the scientists successfully created an antibody to bind with the protein AKT-1. This protein is considered a key player in aging, obesity and cancer, according to the report.

"We're lucky that the first [target] we got is AKT-1," Johnston said.

Now Johnston's research is divided between several different teams, looking at what can be done with the AKT-1 synbody and refining the process of creating antibodies.

"We're already, with AKT-1, exploring [the synbody's] ability to modify to tumor cells," he said.

Theoretically, AKT-1's synbody could be administered to a cancer patient in order to attack the tumor, not unlike the way the antibody Herceptin is used to fight breast cancers.

While the goal of this research, Johnston explained, was to find a cheap, simple way to produce antibodies, it has really opened the doors for biomedical research.

"We're very interested in getting this process ready," said Johnston. "The next big challenge is to make binding agents to all human proteins. We think the importance of this work is that it offers a much simpler, cheaper pathway to making binding agents to human proteins."

Binding agents - ligands - for all of the human proteins, are basic tools for understanding how proteins work, said Johnston.

"Without those agents, we really can't find anything about how proteins really work. It's a critical tool," he said. "Along the way, some binding agents may also be candidates for new therapies or diagnostics."

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