Physics-Biology interface seminar

Using microfluidics for quantitative studies of post-embryonic development in C. elegans

Wolfgang Keil (Institut Curie, Paris)

Special location and time; seminar hosted by Carsten Janke

The development of most metazoans can be divided in an early phase of embryogenesis and a subsequent phase of post-embryonic development. Developmental dynamics during the post-embryonic phase are generally much slower and often controlled by very different molecular mechanisms that, e.g., ensure tissue synchrony and integrate metabolic queues. However, obtaining long-term in-vivo quantitative imaging data post-embryonically with good statistical and cellular resolution has been highly challenging because animals must be allowed to grow, feed, and move in order to properly develop after embryogenesis. In this talk, I will discuss our recent progress in overcoming these challenges in the model organism C. elegans, using microfluidics technology. I will then outline two of our recent studies, in which quantitative in-vivo imaging data of post-embryonic development allows novel insights into mechanisms of cell-fate acquisition and the regulation of oscillatory gene expression in C. elegans.

Stefan Karpitschka (MPI Göttingen)

Heiko Rieger (Saarland University)

Probing proteins in small volumes

Tuomas Knowles (Cambridge University, UK)

This talk outlines our efforts on exploring experimental strategies to provide a new window into protein self-assembly that are enabled by operation in small volumes. We have shown that microconfinement achieved through droplet microfluidics allows the isolation of single nucleation events in protein aggregation and thus to study a rare event as single molecule resolution. Using this strategy we have also been able to develop an understanding of how aberrant misfolded protein states are transmitted from one molecule to another through time and space. More recently we have exploited measurements of mass transport through fluid streams under laminar flow conditions to generate a platform for probing protein-protein interactions under fully native conditions.