biochemistry Platform b & # 39; is strengthening a new robust study & # 39; family & # 39; enzymes are promising targets for cancer treatment.
Today published in Scientific Advances, The new method provides a picture & # 39; high resolution about how these enzymes called methyltransferases lysine, mark b & # 39; selective protein manner & # 39; chemical tags to alter their function. Because of their central role in all aspects of health and disease, proteins and molecules to edit and interact with them are often targets for therapeutic development.
The platform was developed by Scott Rothbart, Ph.D. a & # 39; the Research Institute & # 39; Van Andel, b & # 39; & # 39 collaboration with; EpiCypher, Inc.
"This technology enables us determine the networks & # 39; protein interaction for this family & # 39; widespread enzyme-based chemical labeling," says Rothbart. "Several inhibitors & # 39; these enzymes are currently in the pipeline for clinical development for cancer therapy. Defining the spectrum of their activity is critical to understand exactly how they work these medications and to choose a reliable biomarkers to pursue their activity in & # 39; patients. "
Humans have approximately 20,000 paradise contain instructions for making proteins, the molecular work of the cabins that are responsible for carrying out each process in the human body, to help in the digestion of food to manage the communication between cells.
Once build protein, its function & # 39; often modified by the addition of & # 39; small chemical tags, which instruct proteins the cell where to go and when doing their work. There are over 100 different types of & # 39; these labels, including the addition of & # 39; methyl groups & # 39; amino acid lysine.
Using their new technique, the team found that many other proteins can be labeled by & # 39; methylation of lysine than previously thought.
"Our study suggests that what we know about lysine methylation is just the tip of the iceberg," said Evan Cornett, Ph.D., first author of the study and Postdoctoral fellow in the laboratory a & # 39; Rothbart at the Institute. "The method we have developed allows us to identify new targets in the whole set of & # 39; methyltransferases lysine in humans and, b & # 39; so, help us and others to determine which cancers and other diseases can benefit from targeting treatments for this classroom of & # 39; enzymes. "
This technology is the latest advance comes from a collaboration between laboratory & # 39; Rothbart and EpiCypher. Their work was supported by several grants & # 39; Research of the Small Business Innovation (SBI) by several National Institutes of Health (NIH). Commonly known as the American Seed Fund, providing grants SBIR & # 39; federally funded research to the small businesses in an effort to invest in the discovery led by America. The SBIR program supports small businesses in the biotechnology sector, b & # 39; focus on strategies that have a high potential for significant impact and marketing & # 39; success in the medical field. The SBIR grants recommend more academic-industrial partnerships to bridge the gap between basic science and clinical advances, and are important stimulators of & # 39; technological innovation.
"The beauty of & # 39; this technology is simplicity and its capacity, which is staggering compared to the current mass spectrometry-based approaches," said Martis Cowles, Ph.D., Officer main EpiCypher and co-author of the study. "We are keen to use this technology to help drug developers identify new therapeutic targets and also identify substrates & # 39; optimal target for screening & # 39; & # 39 b inhibitors; high level."
Van Andel Research Institute. .