Dept. of Chemistry and Biochemistry

University of Alaska Fairbanks

PO Box 6160

Fairbanks, AK 99775-6160

(907) 474-5237

ffmks@uaf.edu

Schulte Homepage

After completing his undergraduate work in Natural Science at St. John's University, Minnesota, Marvin Schulte received a M.S. in Biochemistry in 1989 and a Ph.D. in Biochemistry in 1992 from the University of Minnesota.  Following postdoctoral positions at the Medical College of Pennsylvania, he was appointed Assistant Professor at the University of Louisiana at Monroe.  Marvin Schulte joined the University of Alaska Fairbanks as an Associate Professor in 2004.

RESEARCH INTERESTS OF THE SCHULTE  LABORATORY

My laboratory is interested in the structure and function of ligand gated ion channels. Long term goals of the laboratory include elucidation of structural features responsible for ligand binding, channel opening and stabilization of different conformations of these receptors. We are currently focusing on the ligand binding domain of the 5-HT3 receptor. Mutagenesis studies of these receptors have identified several amino acids that appear to interact with ligands, however, specific functional group interactions have not been confirmed. Our research is aimed at identifying the specific amino acids that bind each functional group on the ligand. In collaboration with Dr. Karen Kirschbaum's laboratory, we have developed a series of novel compounds that enable us to probe these interactions. We have successfully identified amino acids that interact with two functional groups of 5-HT3R antagonists and are in the process of refining our knowledge of these interactions. Our future goal is to utilize molecular modelling techniques to determine the 3 dimensional relationships between different interacting amino acids. (This work is supported by a grant from the Southeast Affiliate of the American Heart Association).

A second area of interest centers on the action of general anesthetics on ligand gated ion channels. It is has been demonstrated that many of the effects attributed to general anesthetics are due to their direct interaction with this class of receptor proteins. General anesthetics exhibit a wide range of effects on ligand gated ion channels including alterations in desensitization rates, ion conductance and agonist affinities. Determination of the specific molecular mechanism of general anesthetics will increase our knowledge about the basic functional properties of ligand gated ion channels and provide more insight into potential complications resulting from administration of these commonly used drugs. This research will also provide drug developers with important information that can be used to develop better drugs with fewer side effects, thus reducing the risks to patients. (This work is supported by a grant from the National Science Foundation).

SELECTED PUBLICATIONS

Zhang, Y; Venkatachalan, SP; Xu H; Xu, X; Joshi, P; Ji, HF and Schulte MK. “Binding-Driven Micromechanical Motion for Novel         Label-free Drug Discovery.” Biosensors and Bioelectronics. In Press (2003).

Joshi, P and Schulte MK. “A Vertical Flow Chamber for Xenopus Oocyte Electrophysiology and Automated Drug Screening.” Journal of Neuroscience Methods. In Press (2003).

Schulte, MK. “A Team Based Approach to Integrating Secondary and Post-secondary Students Into Ongoing Laboratory Research.” Journal of Pharmacy Teaching. In Press (2003)

Venkataraman, P; Joshi, PR; Ma, C; Parihar, HS, Kirschbaum KE and Schulte MK. “Functional Group Interactions of a 5-HT3R Antagonist.” BMC-Biochemistry. 3(1):16 (2002).

Venkataraman, P, PV Srinivassan, Muthalagi, M and Schulte, MK “Identification of critical residues in loop E in the 5-HT3ASR binding site”. BMC-Biochemistry. 3(1):15 (2002).

Parihar, HS, Suryanarayanan, A; Ma C; Joshi, PR; Venkataraman, P; Schulte MK and Kirschbaum, KE. “5-HT(3)R Binding of Lerisetron: An Interdisciplinary Approach to Drug-Receptor Interactions." Bioorg Med Chem Lett. 20;11(16):2133-6 (2001).

Yan, D; Schulte, MK; Bloom, KE and White, MM. "Structural Features of the Ligand-Binding domain of the serotonin 5HT3 receptor." Journal of Biological Chemistry, 274,(9) 5537-5541 (1999).