Alexander Kai Buell

2 M DKK to develop a revolutionary new methodology

Monday 21 Sep 20


Alexander Kai Büll
DTU Bioengineering
+45 45 25 40 61

Alexander Kai Büll research group

Application of protein engineering in combination with a wide range of biophysical tools, such as calorimetry, biosensing, fluorescence spectroscopy, AFM and microfluidics for the study of the kinetics and thermodynamics of biomolecular self-assembly.

Protein Biophysics

Villum Experiment

The Villum Experiment Programme has been created for research projects in technical and natural sciences that challenge the norm and have the potential to change the way we approach important subjects. The applicants are anonymous to the international assessors to increase the focus on the research ideas and to let the researchers think freely.

The grant is of DKK 1-2m and runs for up to two years. The programme is announced each year in an open competition with an application deadline in March.

Read more about the Villum Experiment Programme

Villum Experiment grant of 2 M DKK will give a better understanding of the fundamental physics behind an important biological process and its link to some severe diseases.

In this year’s round 51 researchers have received Villum Experiment grants to test their bold and strange research ideas in technical and natural sciences. The projects have been selected from among nearly 500 applications that have been through an anonymous selection process. Professor Alexander Büll is one out of 21 DTU researchers to receive a Villum Experiment grant for the project Massive Exploration of the Sequence Dependence of Protein Phase Separation. He says:

“I am very happy to be able to develop this methodology. It will allow us better to understand the fundamental physics behind an important biological process and its link to some severe diseases. We also hope to employ this methodology for the discovery of new protein sequences that can react to environmental stimuli in a desired way and can be used for biotechnological applications.”

About the project

Protein solutions can spontaneously de-mix and form very concentrated droplets within a background of a very dilute solution: the concentration difference between inside and outside of the droplets can be a factor of 100 or more. This process is called liquid-liquid phase separation (LLPS) and is, for example, the mechanism behind the formation of membrane-less organelles in biology. There is great potential in both medicine and biotechnology in the ability to control this process through external parameters. However, it is currently not well understood how a given protein sequence interacts with the external parameters (pH, temperature, other compounds) to drive LLPS.

Current technology allows to study this phenomenon at a relatively small scale, with ~10 different protein sequences routinely investigated. The aim of this project is to develop a revolutionary new methodology in order to test the LLPS behaviour of, ultimately, millions of times more different protein sequences than is currently possible.

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