CBE Professor Matt DeLisa, the William L. Lewis Professor of Engineering, has been awarded the 2013 AIChE Division 15c Plenary Lecture.
The Food, Pharmaceutical and Bioengineering Division (FP&BE) division (“Division 15”) of the American Institute of Chemical Engineers (AIChE) provides engineers and scientists interested in the field of food, pharmaceuticals, and bioengineering with places to join and to discuss.
Professor Matt DeLisa, the William L. Lewis Professor of Engineering, has been accepted into the 2014-2015 class of the Defense Science Study Group (DSSG).
The DSSG is a program of education and study that introduces selected scientists and engineering professors to the challenges facing national security and encourages them to apply their talents to these issues either as government advisers or in their own research.
Professor Matthew DeLisa was selected as the 2013 Biochemical Engineering Journal Young Investigator.
“This award recognizes outstanding excellence in research and practice contributed to the field of biochemical engineering by a young community member. The award and associated lecture are presented on an annual basis either at the Annual AIChE meeting in conjunction with the FPBE Division (even years) or the ECI Biochemical and Molecular Engineering Conference (odd years).
Back in his days as a Ph.D. student at the University of Maryland, College Park, Matthew P. DeLisa began daydreaming about engineering bacteria to make humanlike glycoproteins that could in turn find use as innovative drugs.
It wasn’t until a decade later, however—as DeLisa joined the faculty of Cornell University’s School of Chemical & Biomolecular Engineering—that he and his group dove into research that began to turn his dreams into reality.
Eager to tap the commercial potential of his glycosylation concept, DeLisa joined with one of his first graduate students, Adam C. Fisher, to form Glycobia in 2009.
“The characteristics that make Matt a good scientist also make him a good entrepreneur. Most important, he has a willingness to take large, calculated risks,” says Fisher, who is Glycobia’s chief science officer. This attitude has served them well while they launched the company, Fisher adds.
Like quality-control managers in factories, bacteria possess built-in machinery that track the shape and quality of proteins trying to pass through their cytoplasmic membranes, Cornell biomolecular engineers have shown.
This quality-control mechanism is found in the machinery of the twin-arginine translocation (TAT) pathway, which is a protein export pathway in plants, bacteria and archaea (single-celled microorganisms). The transport of proteins across cellular membranes is a basic life process and understanding how the TAT pathway works could lend insight into, for example, how bacteria become resistant to antibiotics.
The discovery is a milestone in a 10-plus year study of the TAT pathway led by Matthew DeLisa, associate professor of chemical and biomolecular engineering, and is detailed in Proceedings of the National Academy of Sciences, July 30.
“Our first paper on this topic [PNAS, May 13, 2003] suggested that, given the fact that only folded proteins can go through this system, perhaps a quality-control mechanism was embedded in the machinery itself,” DeLisa said. “That idea turned out to be controversial, but this most recent paper, we think, reopens that possibility.
A method for engineering a bacterial strain to create eukaryotic glycoproteins developed by Professor Matthew DeLisa and colleagues is presented this week in Nature Chemical Biology.
These results may have immediate importance for industrial production of glycoproteins that scientists use in looking for therapies for various diseases.
Several years ago, when Adam Fisher, Ph.D. ’08, was still a graduate student, he and colleagues dreamed up an entirely new way to synthesize human drugs called glycoproteins, which are used to treat a range of conditions from cancer to multiple sclerosis and are a fast-growing corner of the biopharmaceutical industry.
On Feb. 9, a major milestone of that dream was celebrated at the opening of Cornell’s McGovern Family Center for Venture Development in the Life Sciences. Fisher’s company, Glycobia Inc., is the first to rent lab and office space in the center’s business incubator facility. The company moved into the center Jan. 16.
Bringing Glycobia to the McGovern Center, Cornell President David Skorton said, is a "realization of the land-grant mission of Cornell." While it’s one point in the process for sowing the seeds of venture development, Skorton said, it is important to celebrate when the work reaches a certain point, and "today is a big point," he said.
The McGovern Center assists high-potential, early-stage life science spinoff companies that are founded by inventors at Cornell’s Ithaca, Geneva, New York City and Qatar campuses. Its mission is to help young companies prove out their technologies, solidify their management teams, strengthen their business plans and obtain investments to support further growth.
"We’re creating high-tech jobs — life sciences jobs — we’re retaining these jobs, and we’re fostering economic development right here in Ithaca," said Lou Walcer, director of the center.
The science behind Glycobia originated in the lab of Matthew DeLisa, associate professor of chemical and biomolecular engineering, Fisher’s Ph.D. adviser and Glycobia founder.
The company’s product is low-cost "glycoengineering" technology, which works by modifying such common bacteria as E. coli to directly produce human peptide, protein and antibody drugs. Today, protein-based drugs are made by culturing mammalian cells, but this method is costly, time-consuming and hard to control.
"We can make these drugs better," said Fisher, Glycobia’s chief science officer, in his remarks. "We can do things that are simply not possible in any other existing or emerging technology platform."
Glycobia’s bacteria are a manufacturing platform for human therapeutic glycoproteins, which are increasingly becoming a key player in development of drugs to treat a number of diseases. Glycoproteins, DeLisa said, are "regular old proteins" modified at very specific amino acids with sugars. About 70 percent of the human body carries these modifications, so there is a great interest in understanding how they occur.
The idea is to introduce the machinery of glycosylation, which is the process by which proteins are modified by sugar molecules, into the E. coli cells, and to easily go in and tailor the sugar structures for specific applications, DeLisa said.