The image shows a "site-selective" Wacker oxidation on a microelectrode array, fabricated(?) by Kevin Moeller's research group. In this experiment, the Wacker oxidation is triggered by using the electrodes in the array to generate a Pd(II) oxidant.

Three synthetic bacteriochlorins (mauve, gold, teal) are each attached to a native-like bacterial photosynthetic β-peptide (green), which self assembles with α-peptide (blue) and bacteriochlorophyll (purple) to form a dyad (top left) and then a cyclic oligomer with enhanced absorption (lower left).  The three constructs can be combined to give cyclic oligomers (top right) with blended bacteriochlorin absorption (lower right) and ~95% energy-transfer efficiency.

The Mirica group has developed bifunctional compounds that contain both amyloid-binding and metal-chelating molecular motifs. These compounds are efficient inhibitors of the metal-mediated aggregation of the Aβ42 peptide and promote disaggregation of amyloid fibrils. Interestingly, the formation of soluble Aβ42 oligomers in the presence of metal ions and these compounds leads to an increased cellular toxicity.

Using a pulsed laser, the Michael Gross group photolyzes HO-OH to produce HO• for foot printing solvent-accessible side chains on proteins. The approach, coupled with MS analysis, maps protein interfaces faster than a protein can unfold.

Amidine-based catalysts developed by the Birman group show remarkable efficacy and versatility in promoting enantioselective acylation reactions and related transformations. The highly effective kinetic resolution of racemic β-lactam derivatives shown here was achieved by Valentina Bumbu via methanolysis in the presence of (S)-benzotetramisole (BTM).  The resulting enantioenriched protected β-aminoacids may find applications in designing peptidomimetics.

Two new bifunctional compouds that have metal-chelating and amyloid β (Aβ)-interacting groups were synthesized in the Mirica group. The two compounds can promote Aβ42 fibrillization, inhibit Cu2+-induced Aβ42 oligomerization, and reduce their neurotoxicity. Overall, these new bifunctional compounds could be potentially used to control metal-mediated peptide aggregation processes in Alzheimer’s disease.

Faculty, doctoral students and undergraduates talk about the department and their experiences at Washington University. From the outset, students get exposed to a broad range of expertise and fields. Interdisciplinary and collaborative research are strengths of this medium-sized department with considerable resources, instrumentation, and facilities.

The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity has been reported by the Mirica group. A series of biochemical studies reveal that Cu2+ and Zn2+ ions can both inhibit the formation of Aβ42 fibrils. However, while the presence of Cu2+ can lead to the formation of neurotoxic soluble Aβ42 oligomers, the presence of Zn2+ leads to formation of non-toxic Aβ42 aggregates.