Dr. Jonathan Meyers
Indiana University – Bloomington, Indiana
Ph.D. Biological Chemistry Graduated: 09/2012
Dept. of Chemistry, Laboratory of Prof. Richard DiMarchi, (2006 - 2012 )
- Developed a synthetic methodology for the total synthesis of insulin and insulin-like
improved over existing schemes by forming Insulin's three disulfide bonds in two steps and increased the total yield by more than five-fold.
- Determined SAR on the C-domain region of an insulin/IGF-1 hybrid peptide. The work resulted in potent single-chain analogs that were subsequently patented and licensed to Merck research labs.
- Produced biosynthetic and synthetic insulin analogs to study the role of the C-terminal
end of the
insulin receptor's alpha subunit, and resulted in peptides with more than ten-fold greater selectivity for the insulin receptor than native insulin.
University of West Georgia -- Carrollton, Georgia
B.S. Chemistry with ACS certification Graduated: 12/2004
Dept. of Chemistry, Office of Prof. Lucille Garmon (01/2003 - 12/2004)
- Developed a robust rubric that successfully correlated incoming freshmen's high school grade point average, SAT or ACT score and high school transcript to predict success in general chemistry courses at the University of West Georgia. The rubric was presented to the chemistry department for consideration for implementation when the department added remediation courses.
Building upon his graduate research experience, Dr. Meyers has a continued interest in modification of natural peptides as a means of achieving superior pharmacological properties.While all the research in his lab aims to elucidate the underlying links between cancer and diabetes, individual projects falls into two broad categories: a structure activity relationship study of the recently discovered hormone preptin and the development of new methodologies for the biosynthesis of aggregation prone peptides.
Preptin, a 34-amino-acid peptide, is the newest member of the insulin family of peptide hormones, and was isolated from the secretory granules of pancreatic β-cells in 2001 (Figure 1). Since its discovery, it has been broadly implicated as participating in such processes as cellular differentiation, modulation of insulin sensitivity, and regulation of bone density. A search of the literature reveals that only a few analogs of preptin have been reported thus far. Student in his lab are currently undertaking a systematic exploration of the structure activity relationship (SAR) of preptin.
The biosynthesis of recombinant proteins via bacterial expression has proven to be of incalculable value for research and pharmaceutical use. However, not all proteins can be successfully isolated using current expression systems. The formation of inactive, highly ordered, tertiary structures (i.e. fibrils); as well as non-specific aggregation in the cellular system, often reduces the final yield of the active monomeric protein to levels below what is necessary to support biochemical characterization (Figure 2). Student projects are currently focused on using exogenous polyphenols to increase the biosynthetic yield of aggregation prone peptides.
Dr. Meyers grew up in rural Louisiana, and moved to Georgia for the first time in 1998. While living in Carrollton, he attended the University of West Georgia where he earned his B.S. in chemistry. In 2012, he earned his Ph.D. in Chemistry with a focus on chemical biology from Indiana University. At IU he studied under the guidance of Dr. Richard DiMarchi (inventor of the first biosynthetic peptide analog approved by the FDA), and his thesis focused on eliminating the carcinogenic potential of insulin based therapies used for the treatment of Diabetes Mellitus. His research resulted in a patent that was licensed to an international pharmaceutical company, and his insulin analogs are currently being tested in animal models. Dr. Meyers moved to Georgia for the second time in the summer of 2014 to fulfill his long standing goal of becoming a professor at a regional university with a strong commitment to undergraduate research.