个人简介

NIH NRSA Postdoctoral Fellowship, University of Michigan, Ann Arbor, 2009 Goering student fellowship, University of Wisconsin-Madison Chem. Department, 2008 Fulbright Fellowship, Zürich, Switzerland, 2002-2003

研究领域

Chemical Biology/Organic Chemistry/Analytical & Bioanalytical Chemistry

Research in our group focuses on modulating protein-protein interactions through the use of small molecules and bio-inspired peptide scaffolds. By controlling such processes using synthetic molecules that we make in the laboratory, we seek to develop new chemical probes for understanding the underlying biology of protein-protein interactions in disease and ultimately novel therapeutics. Within this interdisciplinary research program, we combine techniques in organic synthesis, biophysics, biochemistry and molecular biology to investigate the folding/misfolding and disease pathways of intrinsically disordered proteins (IDPs). Our research program exploits the bio-orthogonality and the hypersensitivity of fluorine as an NMR probe for exploring important protein-protein interactions of IDPs. Our ultimate goal is to study these proteins in their native environment – whole cells – using 19F NMR. This research is complemented with established spectroscopic techniques, organic synthesis of chemical probes, and new peptide-based strategies for pre-organization and cellular delivery for studying challenging IDPs under physiological conditions.

近期论文

查看导师最新文章 （温馨提示：请注意重名现象，建议点开原文通过作者单位确认）

“Fragment Screening and Druggability Assessment for the CBP/p300 KIX Domain Via Protein Observed 19F NMR” C. T. Gee, E. J. Koleski, W. C. Pomerantz*. Angewandte Chemie Int Ed. 2014 Accepted “Fluorinated aromatic amino acids are sensitive probes for bromodomain ligand interactions”, N. K. Mishra, A. K. Urick, S. W. Ember, E. Schonbrunn, W. C. Pomerantz* ACS. Chem. Biol. 2014 ASAP "FP Tethering: a screening technique to rapidly identify compounds that disrupt protein-protein interactions" J. M. Lodge, J. T. Rettenmaier, J. A. Wells*, W. C. Pomerantz*, A. K. Mapp*, MedChemComm, 2014, 5, 370-375. Recommended for special significance to the field by Faculty of 1000 on F1000prime and among the top ten most downloaded articles in the journal from April to June 2014. "Ordering a disordered protein via a small molecule stabilizer", N. Wang, C. Y. Majmudar,W. C. Pomerantz, J. K. Gagnon, J. D. Sadowsky, J. L. Meagher, T. K. Johnson, J. A. Stuckey, C. L. Brooks III, J. A. Wells, A K. Map p, J. Am. Chem. Soc. 2013, 135, 3363-3366 Featured as a JACS spotlight piece "Sekikaic Acid and Lobaric acid target a dynamic interface of the coactivator CBP/p300" C.Y. Majmudar * J. W. Hojfeldt, * C. Arevang, W.C. Pomerantz, P.J. Schultz, J. K. Gagnon, L. C. Cesa, C. H. Doss, S. P. Rowe, T. Cierpicki, C. L. Brooks III, D. H. Sherman, A. K. Mapp, Ang. Chem. Int. Ed. 2012, 51, 11258 *rated as a "Highly Important Paper" "Profiling the Dynamic Interfaces of Fluorinated Transcription Complexes for Ligand Discovery and Characterization" W.C. Pomerantz , N. Wang; R. Wang, A. K. Lipinksi, T. Cierpicki, A. K. Mapp. ACS. Chem. Biol., 2012, 7, 1345- 50. See "Highlighting our Authors" in the same issue "Lyotropic Liquid Crystals from ACHC-Rich β -peptides", W. C. Pomerantz, V. M. Yuwono, R. Drake, J. D. Hartgerink, N. L. Abbott, S. H. Gellman, J. Am. Chem. Soc. 2011, 133, 13604-13. "Lyotropic liquid crystalline phases from helical β -peptides as alignment media", C. Thiele; W. C. Pomerantz, N. L. Abbott; S. H. Gellman, Chem. Comm., 2011, 47, 502-4 "Transcriptional Tools: Small Molecules for Modulating CBP KIX-dependent Transcriptional Activators", C. A. Bates; W. C. Pomerantz; A. K. Mapp; Biopolymers, 2011, 95, 17-23 "Streamlined monitoring of backbone thioester exchange by 19F NMR" W. C. Pomerantz, *E. B. Hadley, *C. G. Fry, S. H. Gellman, *These authors contributed equally. ChemBioChem 2009,10, 2177-81. "Pre-clinical development of a bi-functional, cancer cell homing, PKC-epsilon in hibitory peptide for treatment of head William Pomerantz, Ph.D Curriculum Vitae 3 and neck cancer." L. W. Bao, M. A. Gorin, M. Zhang, A. C. Ventura, W. C. Pomerantz, S. D. Merajver, T. N. Teknos, A. K. Mapp, Q. Pan Cancer Res. 2009, 69, 5829-34. "Effect of sequence and structural properties on 14-helical β-peptide activity against Candida albicans planktonic cells and biofilms" A. J. Karlsson, W. C. Pomerantz, K. J. Neilsen, S. H. Gellman, S. P. Palecek, ACS Chem. Biol. 2009, 4, 567-79. "A Rationally Designed Aldolase Foldamer" M M. Muller, M. A. Windsor, W. C. Pomerantz, S. H. Gellman, D. Hilvert, Angew. Chem. Int. Ed. 2009, 48, 922-5. "Characterization of nanofibers formed by self-assembly of β-peptide oligomers using small angle x-ray scattering."C. L. Pizzey, W. C. Pomerantz, B.- J. Sung, V. M. Yuwono, J. D. Hartgerink, A. Yethiraj, S. H. Gellman, N. L. Abbott, J. Chem. Phys., 2008, 129,095103-1-8. "Distinctive circular dichroism signature for 14-helix-bundle formation by β-peptides." W. C. Pomerantz, T. L. Grygiel, J. R. Lai, S. H. Gel lman, Org. Lett. 2008, 10, 1799-1802. "Nanofibers and lyotropic liquid crystals from a class of self-assembling β-peptides" W. C. Pomerantz, C. L. Pizzey, V. M. Yuwono, J. D. Hartgerink, N. L. Abbott, S. H. Gellman, Angew. Chem., 2008, 47, 1241-4. "Comparisons of design strategies for promotion of 14-helix stability in water", E. Vaz, W.C. Pomerantz, M. Geyer, S. H. Gellman, L. Brunzveld, ChemBioChem, 2008, 9, 2254-59. "Origins of the high 14-helix propensity of cyclohexyl-rigidified residues in β-peptides."M.- R. Lee, T. L. Raguse, M. Schinnerl, W. C. Pomerantz, X. Wang, P. Wipf, S. H. Gellman, Org. Lett. 2007, 9, 1801-4. "Sequence dependent behavior of amphiphilic β-peptides on gold surfaces."W. C. Pomerantz, K. D. Cadwell, Y.-J. Hsu, S. H. Gellman, N. L. Abbott, Chem. Mater. 2007, 19, 4436-41. "Practical synthesis of enantiomerically pure β-amino acids via proline-catalyzed diastereoselective aminomethylation of aldehydes." Y. Chi, E. P. English, W. C. Pomerantz, W. S. Horne, L. A. Joyce, L. R. Alexander, W. S. Fleming, E. A. Hopkins, S. H. Gellman, J. Am. Chem. Soc. 2007, 129, 6050-5.