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.
Department of Chemistry · UC Irvine
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
We design constrained peptides derived from Aβ and other amyloidogenic proteins, then determine the structures of the toxic oligomers they form.
Our oligomer mimics raise conformation-selective antibodies that recognize pathological Aβ and protect neurons, a route toward better probes and treatments.
We synthesize teixobactin, clovibactin and related antibiotics, then build analogues, prodrugs and conjugates that are more potent and easier to use.
Fluorescent analogues and X-ray crystallography let us watch teixobactin assemble on the bacterial surface and attack the cell envelope on two fronts.
β-Sheets connect both programs. The same supramolecular chemistry that drives amyloid oligomers also governs how teixobactin assembles to kill bacteria.
X-ray crystallography and solution-phase NMR let us see these assemblies directly. Our structures are deposited in the Protein Data Bank.
Latest from the lab
Org. Biomol. Chem. 2025, 23, 3881–3893.
J. Org. Chem. 2025, 90 (5), 2132–2136.
Group life
James presenting at the American Chemical Society Fall 2025 meeting in Washington, D.C.
Nowick alumni and group members at the American Peptide Symposium 2025.
Group lunch at Onotria in Costa Mesa.