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Mark Young in his lab in Montana State's Agricultural Bioscience Building.

A decade-long collaboration that began from examining the protein function of viruses has yielded the technology to use viruses as containers for helping the body, rather than harming it. Professors Trevor Douglas and Mark Young saw the possibilities of viruses working as containers for inorganic material and have proven an effective method to redesign viruses and activate protein cages to work as molecule delivery systems. Basically, using the protein cage architecture, synthetic cargos take a ride on the backs of viruses undetected by the rest of the body. The cages can be controlled to release therapeutic agents directly at a target, consequently reducing negative side effects.

"This is an exciting development because we can change viruses from disease causing agents to disease-prevention agents," said Mark Young, PhD, a biochemist at the University of California-Davis, in article he coauthored with Douglas in a recent edition of the journal Science. "We expanded this approach to use other protein cage architectures to encapsulate and deliver a range of useful molecules."

Armed with their new development, Young and Douglas became scientific co-founders of a new Montana biotechnology company, SpeciGen, which will manufacture the protein cages for distribution and marketing to researchers.

"We do have natural protein cages that store iron (ferritin)," explains Trevor Douglas, PhD, a chemist at Montana State University. "We're taking basic science and applying it to make the viruses do what we want them to do."

Not only can imaging and therapeutic agents be encapsulated in the protein cages, but the cages can be given a targeting agent, an antibody or peptide, known as a "zip code," which then bonds to a particular cell type and can be directed to a specific disease site.

SpeciGen is currently interested in cancer therapy, and officials are in talks with pharmaceutical research teams to use the protein cages in three different applications. If a company has a relatively new drug and has been working to develop a second generation of that drug, the protein cage is a viable option to improve its efficacy. It can also be used to make soluble drugs that were previously insoluble, and protein cages could mean a new shelf life for expired or soon-to-be expired drugs. Offering a range of protein cage sizes from 9 nm in diameter and upward, SpeciGen officials explain, there are distinct advantages in getting the protein cage and drug shipment where the drug is needed.

"The real advantage of this over existing technology is all viruses in the population are the same," says Douglas, explaining that typically viruses are seen as one big molecule, but with the protein cage development, the location of every atom in the molecule is known. "It's taking it and giving it atomic level control, which is not true of liposomes."

SpeciGen CEO Lonnie Bookbinder contends the platform for these protein cages is broad and deep, with the ability to cover a wide variety of diseases and drugs.

"The utility of this approach has been demonstrated with the use of our library of cages to attach and selectively release the anticancer drug, doxorubicin," Bookbinder says. "Targeted delivery is medically advantageous because our protein cages allow us to sequester the cargo until delivered and directed to release the drug in a specific physiological environment."

While there is no reason the protein cages can't theoretically work for all diseases, Douglas says, they will probably find a niche. Ultimately, the protein cage delivery systems may
lead to major benefits in drug therapy, such as fewer side effects and improved effectiveness.

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