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Paul T. Wilder, PhD

Academic Title:

Assistant Professor

Primary Appointment:

Biochemistry and Molecular Biology

Additional Title:

Section Leader, Target Validation and Screening, Center for Biomolecular Therapeutics


Biomedical Research Facility (BRF) 108 N. Greene St., Room 429

Phone (Primary):

(410) 706-5003

Education and Training

  • Worcester Polytechnic Institute, BS, Biotechnology, 1993
  • University of Maryland School of Medicine, PhD, 2004
  • University of Maryland School of Medicine, Postdoctoral Fellowship, 2008


Dr. Wilder is the University of Maryland School of Medicine Center for Biomolecular Therapeutics (CBT) Target Validation & Screening Section (TVS) Leader.  The CBT TVS has the technical expertise, equipment such as automated liquid handling stations, and compound libraries necessary to validate drug targets, develop screening assays, and find small molecule perturbagens that may lead to new therapeutics.  They also assist in the development and testing of biologic therapies such as therapeutic antibodies, stabilized peptides and peptidomimetics, and developing methods to get therapeutic proteins intracellularly.  The majority of the projects use structure based drugs design, protein and compound structure using both NMR and X-ray crystallography, to either create or improve compound affinity and specificity.  In addition, uses cell engineering techniques such as CRISPR to create novel cellular assays and models for developing and testing putative therapeutics.  While many of the projects are aimed at developing cancer therapeutics there are additional projects working on antivirals, antibacterials, and diabetes.

In his previous work, Dr. Wilder acquired a broad scientific background in both academia research and industrial biotechnology.  In his industrial experience, he developed and performed assays to assure the purity and efficacy of both biologic and cellular therapeutics using ELISA, FACS, cell separation/purification, fluorescence microscopy, and stem cell culture.  In his Ph.D. training, he performed biochemical and biophysical studies using a wide range of techniques including protein structural studies, cellular and molecular biology including NMR, fluorescence spectrophotometry, ITC, and protein purification.  In his postdoctoral training he focused on structural based drug design and high throughput screening (HTS) aimed at developing new therapeutics for treating malignant melanoma.

Research/Clinical Keywords

High-throughput screening (HTS), structural biology, drug discovery, cancer biology, biophysic, protein chemistry, fluorescence spectroscopy, cell and molecular biology, zinc, calcium, assay development, cell signaling

Highlighted Publications

Wilder, P.T., Vallely, K.M., Weiss, M.B., Gitti, R.K., Weber, D.J. (2005) Solution structure of zinc and calcium-bound rat S100B as determined by nuclear magnetic resonance spectroscopy.  Biochemistry 44, 5690-5702.

Wilder, P.T., Charpentier, T.H., Liriano, M.A., Gianni, K., Varney, K.M., Pozharski, E., Coop, A., Toth, E.A., MacKerell, A.D., Weber, D.J. (2010) In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction.  International Journal of High Throughput Screening 2010(1):109-126.  PMCID:  PMC2995924

Ramagopal, U.A., Dulyaninova, N.G., Varney, K.M., Wilder, P.T., Nallamsetty. S, Brenowitz, M, Weber, D.J., Almo, S.C., Bresnick, A.R. (2013) Structure of the S100A4/myosin-IIA complex.  BMC Structural Biology 13:31.  PMCID: PMC3924328

Hartman, K.G., Vitolo, M.I., Pierce, A.D., Fox, J.M., Shapiro, P., Martin, S.S., Wilder, P.T., Weber, D.J. (2014) Complex Formation Between S100B and the p90 Ribosomal S6 Kinase (RSK) in Malignant Melanoma is Ca2+-dependent and inhibits ERK-mediated Phosphorylation of RSK.  J. Biol. Chem 289(18):12886-95. PMCID: PMC4007476

Lanning, M.E., Yu, W, Yap, J.L., Chauhan, J, Chen, L, Whiting, E, Pidugu, L.S., Atkinson, T, Bailey, H, Li, W, Roth, B.M., Hynicka, L, Chesko, K, Toth, E.A., Shapiro, P, MacKerell, A.D. Jr, Wilder, P.T., Fletcher, S. (2016)  Structure-based design of N-substituted 1-hydroxy-4-sulfamoyl-2-naphthoates as selective inhibitors of the Mcl-1 oncoprotein.  Eur. J. Med. Chem. May 4; 113: 273-292.