Organic and Bioorganic Chemistry, Chemical Biology
•Charles R. Bennett Service Through Chemistry Award from the ACS Orange County Section
•American Chemical Society (ACS) Fellow
•American Association for the Advancement of Science (AAAS) Fellow
•NOGLSTP Scientist of the Year Award
•UCI School of Physical Sciences Award for Outstanding Contributions to Undergraduate Education
•American Chemical Society Arthur C. Cope Scholar Award
•UCI Chancellor's Award for Excellence in Undergraduate Research
•Alfred P. Sloan Research Fellowship
•Camille Dreyfus Teacher-Scholar Award
•Presidential Faculty Fellow
•UCI Award for Outstanding Faculty Contribution to Undergraduate Research
•Arnold and Mabel Beckman Foundation Young Investigator
•National Science Foundation Young Investigator
•American Cancer Society Junior Faculty Research Award
•Camille and Henry Dreyfus Foundation Distinguished New Faculty Award
•National Science Foundation Postdoctoral Fellow
•American Chemical Society Division of Organic Chemistry Graduate Fellow
•National Science Foundation Graduate Fellow
Postdoctoral Fellow, M. I. T.
Joined UCI faculty in 1991
Research in the Nowick group focuses on the chemistry and biology of peptides. Areas of particular interest include understanding molecular basis of amyloid diseases, such as Alzheimer’s disease, and the development of new antibiotics.
The design, synthesis, and study of new molecules is central to our efforts. We use small molecule chemical synthesis, peptide synthesis, and protein expression to create the molecules that we study, and molecular modeling, NMR spectroscopy, and X-ray crystallography to gain insights into their structures and biomolecular interactions. Experiments with mammalian cells and bacteria, as well as fluorescence microscopy help elucidate the biological properties of the molecules that we create, as do some animal-based studies in mice. A particular area of interesting our laboratory is the structures and supramolecular interactions of ß-sheets, which are central to the folding and assembly of the peptides associated with amyloid diseases, such as Alzheimer’s disease, as well as the antibiotic teixobactin.
Our extensive program of research on understanding the molecular basis of amyloid diseases focuses on developing chemical models of the toxic amyloid oligomers associated Alzheimer’s disease and other amyloid diseases. In typical studies, we design peptides derived from Aß and other amyloidogenic peptides and proteins and then study their structures and assembly, as well as their biological properties. Through X-ray crystallography, we have been able to observe the structures of a variety oligomers formed by constrained ß-hairpin peptides derived from key amyloidogenic peptides and proteins. Current efforts seek to correlate these chemical models of amyloid oligomers with biogenic amyloid oligomers found in the brain and to develop antibodies and vaccines to block the neurodegeneration associated with these amyloid oligomers.
In 2015 we became interested in the newly reported antibiotic teixobactin and launched a program of study to learn more about its chemistry and biology. By synthesizing teixobactin analogues and studying their antibiotic activity, we gained new insights into the mechanism of action of teixobactin. Through X-ray crystallography, we discovered that teixobactin forms dimers and higher-order assemblies through ß-sheet formation that can bind to its molecular targets on the cell membrane of Gram-positive bacteria. We are now using what we have learned from teixobactin to design new antibiotics against MRSA, VRE, and other dangerous pathogens.
Students in the Nowick group partake fully of the rich environment of mentorship and training provided by our research laboratory. Graduate students participate in hypothesis generation, data collection, data analysis, and communication through oral and written presentation. Many graduate students choose to mentor undergraduate research students, further enhancing their graduate training while helping to train the next generation. I meet with students individually each week to discuss their results and plans for subsequent experiments. Additional scheduled and ad-hoc meetings occur throughout the week. When students are writing papers for publication, I work closely with them, providing guidance and feedback in the writing process.
My group and I meet collectively on Tuesday afternoons during our weekly group meetings. Our group meetings consist of three formats: research, literature, and workshop. In our research group meetings, students present and discuss their results orally with slides and get feedback and discussion that leads to ideas for future experiments. In our literature group meetings, we discuss important publications from the current literature, with each student making slide presentations on articles. When students are preparing to give talks or engaging in various writing projects, the group often provides feedback and guidance in a workshop format. Through this program of research training, continuing education, and mentorship, students acquire the skills to become successful independent scientists.
Nowick Group Website
Chao Family Comprehensive Cancer Center (UCI)
Institute for Genomics and Bioinformatics (UCI)
Alzheimer's Disease Research Center, UCI MIND (UCI)
Course Video Lectures on YouTube
Chem 203. Organic Spectroscopy, Fall 2020
Chem 203. Organic Spectroscopy, Fall 2020 Course Website
Chem 203. Organic Spectroscopy, Fall 2011
Chem 125. Advanced Organic Chemistry
Chem 51A. Organic Chemistry
Chem 51B. Organic Chemistry (Professor David Van Vranken)
Chem 51C. Organic Chemistry
Links to other OpenChemistry Lecture Videos
Organic Spectroscopy Problems
Link to The UCI Chemistry Outreach Program Web Page
"Mechanism of IAPP Amyloid Fibril Formation Involves an Intermediate with a Transient β-Sheet"
Buchanan, L. E.; Dunkelberger, E. B.; Tran, H. Q.; Cheng, P.-N.; Chiu, C.-C.; Cao, P.; Raleigh, D. P.; de Pablo, J. J.; Nowick, J. S.; Zanni, M. T. Proc. Natl. Acad. Sci. U. S. A. 2013
"Out-of-Register β-Sheets Suggest a Pathway to Toxic Amyloid Aggregates"
Liu, C.; Zhao, M.; Jiang, L.; Cheng, P.-N.; Park, J.; Sawaya,. M. R.; Pensalfini, A.; Gou, D.; Berk, A. J.; Glabe, C. G.; Nowick, J. S.; Eisenberg, D. Proc. Natl. Acad. Sci. U. S. A. 2012
"Macrocyclic β-Sheet Peptides that Inhibit the Aggregation of a Tau-Protein-Derived Hexapeptide"
Zheng, J.; Liu, C.; Sawaya, M. R.; Vadla, B.; Khan, S.; Woods, R. J.; Eisenberg, D.; Goux, W. J.; Nowick, J. S. J. Am. Chem. Soc. 2011
"Cyclic Modular β-Sheets"
Woods, R. J.; Brower, J. O.; Castellanos, E.; Hashemzadeh, M.; Khakshoor, O.; Russu, W. A.; Nowick, J. S. J. Am. Chem. Soc. 2007
"A Ribozyme with Michaelase Activity: Synthesis of the Substrate Precursors" Eisenführ, A.; Arora, P. S.; Sengle, G.; Takaoka, L. R.; Nowick J. S.; Famulok, M. Bioorg. Med. Chem. 2003, 11, 235-249.
"An Unnatural Amino Acid that Induces β-Sheet Folding and Interaction in Peptides"
, Nowick, J. S.; Lam, K. S.; Khasanova, T. V.; Kemnitzer, W. E.; Maitra, S.; Mee, H. T.; Liu, R. J. Am. Chem. Soc. 2002
"Three-Stranded Mixed Artificial β-Sheets" Nowick, J. S.; Smith, E. M.; Ziller, J. W.; Shaka, A. J. Tetrahedron 2002, 58, 727-739.
"Novel RNA Catalysts for the Michael Reaction" Sengle, G.; Eisenführ, A.; Arora, P. S.; Nowick, J. S.; Famulok, M. Chemistry & Biology 2001, 8, 459-473.
"β-Sheet Interactions Between Proteins"
, Maitra, S.; Nowick, J. S. In: The Amide Linkage: Structural Significance in Chemistry, Biochemistry, and Materials Science
; Greenberg, A.; Breneman C. M.; Liebman, J. F., Eds.; Wiley: New York, 2000; Chapter 15.
"An Efficient Synthesis of N,N'-Linked Oligoureas" Wilson, M. E.; Nowick, J. S. Tetrahedron Lett. 1998, 39, 6613-6616.
"Synthesis of Peptide Isocyanates and Isothiocyanates"
, Nowick, J. S.; Holmes, D. L.; Noronha, G.; Smith, E. M.; Nguyen, T. M.; Huang, S.-L. J. Org. Chem. 1996
, 3929-3934. Addendum: J. Org. Chem. 1998, 63, 9144.
"An Artificial β-Sheet Comprising a Molecular Scaffold, a β-Strand Mimic, and a Peptide Strand"
, Nowick, J. S.; Holmes, D. L.; Mackin, G.; Noronha, G.; Shaka, A. J.; Smith, E. M. J. Am. Chem. Soc. 1996