Members of the Nowick Research Group photographed together at UC Irvine, September 2026.

Department of Chemistry · UC Irvine

The chemistry and biology of peptides,
from Alzheimer’s to antibiotics.

We study how peptides fold, assemble, and behave in cells and bacteria. We design β-hairpin peptides as chemical models of the amyloid oligomers associated with Alzheimer's disease, and we synthesize antibiotics such as teixobactin and clovibactin to work out how they kill antibiotic-resistant bacteria.

What we work on

Our research

All research
Ribbon diagrams and sequence schematics of constrained beta-hairpin peptides derived from the amyloid-beta sequences LVFFAED and VMLGIIA.

Amyloid oligomers and Alzheimer’s disease

We design constrained peptides derived from Aβ and other amyloidogenic proteins, then determine the structures of the toxic oligomers they form.

Two triangular trimer mimics derived from amyloid-beta, each leading to a conformation-selective antibody.

Antibodies and immunotherapy

Our oligomer mimics raise conformation-selective antibodies that recognize pathological Aβ and protect neurons, a route toward better probes and treatments.

Chemical structure of an isobactin analogue above a microplate assay showing its minimum inhibitory concentration against MRSA.

Making peptide antibiotics

We synthesize teixobactin, clovibactin and related antibiotics, then build analogues, prodrugs and conjugates that are more potent and easier to use.

Chemical structure of a labeled teixobactin analogue above four fluorescence micrographs of bacterial cells in cyan, green, red and magenta.

How these antibiotics kill bacteria

Fluorescent analogues and X-ray crystallography let us watch teixobactin assemble on the bacterial surface and attack the cell envelope on two fronts.

Schematic of an antiparallel beta-hairpin showing two beta-strands joined by a turn and linked by hydrogen bonds, beside a space-filling molecular model.

β-Sheet chemistry and assembly

β-Sheets connect both programs. The same supramolecular chemistry that drives amyloid oligomers also governs how teixobactin assembles to kill bacteria.

Ramachandran plots beside cyan and green crystal structures of a beta-hairpin peptide and the triangular trimer it assembles into, with bound ions shown as magenta spheres.

Structure by X-ray and NMR

X-ray crystallography and solution-phase NMR let us see these assemblies directly. Our structures are deposited in the Protein Data Bank.

154 Publications since 1984
38 Structures in the PDB
171 Group alumni
1991 At UC Irvine since

Latest from the lab

Recent publications

All publications

Group life

Latest news

All photos
James Nowick giving a lecture beside a projected slide on amyloid oligomer mimics and cyclic depsipeptide antibiotics.
18 August 2025

James presenting at the American Chemical Society Fall 2025 meeting in Washington, D.C.

Four Nowick group members and alumni seated together in a lecture hall at the American Peptide Symposium.
19 June 2025

Nowick alumni and group members at the American Peptide Symposium 2025.

Nowick group members seated around a long table at a restaurant for a group lunch.
18 March 2025

Group lunch at Onotria in Costa Mesa.