John Tomich

Professor of Biochemistry

The Tomich laboratory designs and characterizes synthetic peptides for potential uses as drugs or renewable biomaterials. The lab employs a number of biologic, synthetic, analytic and physical methods to make these characterizations.

B.A. 1974, University of Connecticut
M.S. 1975, Purdue University
Ph.D. 1980, University of Waterloo

Phone: 785-532-5956
Fax: 785-532-7278
Email: jtomich@ksu.edu
Office: 206 Burt Hall

Three projects are being studied by the members of the Tomich Lab. 1) Design, synthesis and testing of anion selective channel forming peptides to determine the mechanism by which channels can show ion selective and still have extremely high transport rates. The object of this research is to develop a sequence that could be used to provide a new chloride conductive pathway in cystic fibrosis patients.  2) Characterization of a peptide that causes a transient yet repeatable disruption of tight junctions in barrier membranes. The goal of this project is to test this peptide’s ability to open barrier membranes and facilitate drug delivery.  3) Design and synthesis of peptides with unusually high adhesive strength. The goal of this project is to design a biodegradable protein sequence that could be introduced and ultimately harvested from crop plants for use in the plywood industry.

Click here for a more detailed description of the research interests of Professor Tomich's labs.

Selected Publications

Broughman, J.R., K. Mitchell, T. Iwamoto, B.D. Schultz, J.M. Tomich. (2001) Amino-terminal modification of a channel-forming peptide increases capacity for epithelia anion secretion. Am. J. Physiol:  (Cell Physiol. )280: C451-458.

Broughman JR, Shank LP, Takeguchi W, Iwamoto T, Mitchell KE, Schultz, BD and Tomich JM. (2002) Distinct structural elements that direct solution aggregation and membrane assembly in the channel forming peptide M2GlyR. Biochemistry  41,7350-7358.

Broughman JR, Brandt, R., Hastings C, Iwamoto T, Tomich JM and Schultz BD, (2004)   Anion Channel-Forming Peptide Modulates Transepithelial Electrical Conductance and Solute Permeability Am. J. Physiol:  (Cell Physiol. )286: C1312-1323.

Cook GA, Prakash O, Zhang K, Shank LP, Robbins, A, Gong Y-X, Iwamoto T, Schultz, BD and Tomich JM. (2004) Activity and Structural Comparisons of Solution Associating and Monomeric Channel-Forming Peptides Derived from the Glycine Receptor M2 Segment. Biophysical J. 86: 1424-1435.