Eckerd College - on Florida's Gulf Coast
Chemistry Department
The Chemistry Department at Eckerd College offers Bachelor's degrees in chemistry, including a chemistry degree certified by the American Chemical Society (ACS). We are one of only two Florida colleges where a student can earn an ACS-certified biochemistry degree.

Dr. Wayne C. Guida

Emeritus Professor of Biochemistry
Office: SHC-211
(727) 864-8993
guidawc@eckerd.edu

Dr. Guida earned his undergraduate and Ph.D. degrees from the University of South Florida. After postdoctoral work at Duke University, he joined the Eckerd College faculty for the first time in 1976. He remained at Eckerd until 1985, where he and his students published papers describing their research in organic chemistry. He then became a Senior Research Associate at Columbia University, working in the area of computational chemistry, and later joined Ciba Pharmaceuticals in Summit, New Jersey where he was responsible for a structural biochemistry and biochemical profiling group. Dr. Guida returned to Eckerd College in 1999 to teach biochemistry. His recent research has focused on structure-based enzyme inhibitor design using computational and experimental methods.

Dr. Guida now works as a Professor of Chemistry at the University of South Florida. 

Dr. Guida

Research Interests:

Our research involves structure-based enzyme inhibitor design, computer algorithms for flexible docking, and binding affinity prediction. Our most recent work involves the design of inhibitors of thymidine phosphorylase, S-adenosylmethionine decarboxylase, Farnesyl Transferase and the Proteasome, all of which may have therapeutic utility in the treatment of cancer. We are also interested in zinc metalloprotease model systems.

An inhibitor of farnesyl transferase docked to the catalytic site of the enzyme. Farnesyl pyrophosphate is also shown (gray).

Guida Molecule
Recent Publications:

1. "Design of Novel N-(2,4-Dioxo-1,2,3,4-tetrahydro-thieno[3,2-d] pyrimidin-7-yl)-guanidines as Thymidine Phosphorylase Inhibitors, and Flexible Docking to a Homology Model", Price, M. L. P.; Guida, W. C.; Jackson, T. E.; Nydick, J. A.; Gladstone, P. L.; Juarez, J. C.; Donate, F.; Ternansky, R. J. Bioorg. Med. Chem. Lett. 2003, 13, 107.

2. "Chemosensors for the Marine Toxin Saxitoxin", Gawley, R.E., Pinet, S., Cardona, C. M., Probal, D. K; Tong, R.; Guida, W. C., Nydick, J.; Leblanc, R. M. J. Am. Chem. Soc. 2002, 124, 13448.

3."Accurate Prediction of Acidity Constants in Aqueous Solution via Density Functional Theory and Self-Consistent Reaction Field Methods", Klicic, J. A.; Friesner, R. A.; Liu, S-Y.; Guida, W. C. J. Phys. Chem. 2002, 106, 1327.

4."Low-mode Conformational Search Elucidated. Application to C39H80 and Flexible Docking of 9-Deazaguanine Inhibitors to PNP" Kolossvary, I.; Guida, W. C. J. Comput. Chem. 1999, 20, 1671.

5. "Guidelines for Publication of Research Results from Force Field Calculations" Raber, D. J; Guida, W. C. Pure and Applied Chemistry 1998, 70, 2047. Kolossvary, I.; Guida, W.C. "Conformational Analysis: 1", in The Encyclopedia of Computational Chemistry; Schleyer, Allinger, Clark, Gasteiger, Kollman, Schaefer & Schreiner, Eds., John Wiley & Sons: New York, 1998.

6. "Purine Nucleoside Phosphorylase. Catalytic Mechanism" Erion, M. D.; Stoeckler, J. D.; Guida, W. C.; Walter, R. L.; Ealick, S. E. Biochemistry 1997, 36, 11735.

7. Babu, Y. S.; Montgomery, J. A.; Bugg, C. E.; Carson, W. M.; Narayana, S. V. L.; Cook, W. J.; Ealick, S. E.; Guida, W. C.; Erion, M. D.; Secrist, J. A. "Design of Purine Nucleoside Phosphorylase Inhibitors" in Structure-Base Drug Design, Veerapandian, P., Ed., Marcel Dekker, Inc.: New York, 1997.

8. "Low Mode Search. An Efficient, Automated Computational Method for Conformational Analysis: Application to Cyclic and Acyclic Alkanes and Cyclic Peptides" Kolossvary, I.; Guida, W. C. J. Am. Chem. Soc. 1996, 118, 5011.

9. "The Art and Practice of Structure-Based Drug Design: A Molecular Modeling Perspective" Bohacek, R. S.; McMartin, C.; Guida, W. C. Medicinal Research Reviews 1996, 16, 3.

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