A Part of the University of Maryland Medical Center

Connect with UMGCC
Facebook Twitter YouTube Blog iPhone
Email PageEmail page Print PagePrint page

Researcher Information

Paul Wilder, Ph.D.
Research Associate

Biochemistry and Molecular Biology

UMGCC Research Program:
Molecular and Structural Biology Program

College Degree: B.S., Worcester Polytechnic Institute
Ph.D., University of Maryland, Baltimore
Post Doctoral Degree: University of Maryland, Baltimore

Contact Information:

Mailing Address: University of Maryland, Baltimore
Bio-Medical Research Facility
108 N. Greene St.
Room 439
Baltimore, MD 21201
Email: pwild001@umaryland.edu
Phone: (410) 706-4353
Fax: (410) 706-0458

Research Interests:
As the associate director of the UMGCC High Throughput Screening Shared Service (HTS SS) my main concern is the day to day operations of the facility. It is my job to use my expertise to assist investigators in the development and adaptation of their specific assays into an automated format with the goal of discovering novel therapeutics for treating diseases and cancers using the automated liquid handling equipment, fluorescent plate readers, and a library of over 54,000 small compounds available in the facility. As such my interests include all aspects of drug discovery and the various related cellular and in vitro techniques.

My background is split evenly between the biotechnology industry working on biologics and cellular therapeutics for about 7 years, and academia working in the laboratory of UMGCC researcher Dr. David Weber. In industry I worked on a carbohydrate based immune-modulator, and on a system for the expansion of cord blood derived stem cells gaining proficiency in assay development in including cell based and ELISA, tissue culture, FACS, magnetic based and other cell separation/purification techniques, and stem cell culture.

In my Ph.D. training I performed biochemical and biophysical studies using a wide range of techniques including NMR, fluorescence, ITC, and protein purification as well as cellular and molecular biology techniques to study the interaction of p53 with the calcium binding protein S100B. During my postdoctoral training I focused on structural based drug design and HTS for breaking the S100B-p53 interaction to provide treatment for cancer that have elevated S100B levels such as melanoma, and glioblastoma.

Charpentier, T.H., Wilder P.T., Liriano, M.A., Varney, K.M., Zhong, S., Coop, A., Pozharski, E., MacKerell, A.D. Jr., Toth, E.A., Weber, D.J. (2009) Small molecules bound to unique sites in the target protein binding cleft of calcium-bound S100B as characterized by nuclear magnetic resonance and X-ray crystallography. Biochemistry 48(26): 6202-6212.

Wright, N.T., Cannon, B.R., Wilder, P.T., Morgan, M.T., Varney, K.M., Zimmer, D.B., Weber, D.J. (2009) Solution structure of S100A1 bound to the CapZ peptide (TRTK12). J. Mol. Biol. 386(5): 1265-1277.

Charpentier, T.H., Wilder, P.T., Lirian, M.A., Varney, K.M., Pozharski, E., Mackerell, A.D. Jr., Coop, A., Toth, E.A., Weber, D.J. (2008) Divalent Metal Ion Complexes of S100B in the Absence and Presence of Pentamidine. J. Mol. Biol. 382(1): 56-73.

Malashkevich, V.N., Varney, K.M., Garrett, S.C., Wilder, P.T., Knight, D., Charpentier, T.H., Ramagopal, U.A., Almo, S.C., Weber, D.J., Bresnick, A.R. (2008) Structure of Ca2+ bound S100A4 and its interaction with peptides derived from nonmuscle myosin-IIA. Biochemistry 47(18): 5111-5126.

Wilder, P.T., Charpentier, T.H., Weber, D.J. (2007) Hydrocarbon-Stapled Helices: A Novel Approach from Blocking Protein-Protein Interaction. ChemMedChem 2(8), 1149-1151.