Laboratory for bioanalytical chemistry

NematodesNematode tracks on a film of E. coli

The laboratory of bioanalytical chemistry develops novel analytical techniques to decipher the ecology and evolution of small molecule signaling and secondary metabolism in nematodes (roundworms).


"In short, if all the matter in the universe except the nematodes were swept away, our world would still be dimly recognizable, and if, as disembodied spirits, we could then investigate it, we should find its mountains, hills, vales, rivers, lakes, and oceans represented by a film of nematodes. The location of towns would be decipherable, since for every massing of human beings there would be a corresponding massing of certain nematodes. Trees would still stand in ghostly rows representing our streets and highways. The location of the various plants and animals would still be decipherable, and, had we sufficient knowledge, in many cases even their species could be determined by an examination of their erstwhile nematode parasites." (Nathan Augustus Cobb, 1915).


Latest Lab News

September 2020

Swiss National Science Foundation grant application funded. The SNF will provide 4 years of support for a research project linking lipogenesis and ascaroside signaling in the model organism C. elegans.

June 2020

Our manuscript describing the characterization of homo- and heterodimeric 2’- and 4’-isomeric ascaroside dimers from bacterivorous Caenorhabditis nematodes has been published in Organic Biomolecular Chemistry. We utilized a combination of HPLC-MS/MS precursor ion scanning, HR-MS/MS, and NMR techniques to identify a variety of dimeric ascarosides from Caenorhabditis remanei and Caenorhabditis nigoni. Structure assignments were confirmed by total synthesis of representative examples. Their biological functions were evaluated using a retention assay that indicated that males of C. remanei and C. nigoni are retained by their conspecific ascaroside dimers but not by the heterospecific isomers. These results demonstrate that dimerization of conserved monomeric ascaroside building blocks dramatically increases structural diversity and represents an efficient mechanism to generate species-specific ascaroside signals in the Caenorhabditis.