2 Post-doc positions – heterotypic amyloid interactions

Updated: about 1 month ago

We recently secured NIH funding for a project investigating heterotypic amyloid interactions as modulators of selective cellular vulnerability. We’re looking for two experienced postdoctoral researchers with strong backgrounds in cell biology and biophysics, both within a protein aggregation context.


What is the project all about?

Amyloid aggregates form in certain regions of the brain and not in others. We will investigate whether specific (heterotypic) interactions between the aggregation-prone regions of amyloid-forming proteins and the background proteome account for this. This hypothesis will be tested by performing a genome-wide computational screen and then testing the candidate proteins first in cellular models and then in mice. Biophysical analyses will shine a light on the exact mechanism by which heterotypic interactions change amyloid formation.


About the lab

The SWITCH Laboratory is a leader in the field of protein aggregation research related to human disease. We are an interdisciplinary workplace, bringing together more than twenty-five researchers from different backgrounds, such as bioinformatics, biophysics, chemistry and cell biology. SWITCH has a unique platform of technologies for studying protein aggregation, including biophysical, ultrastructural and cell biological instrumentations. You can read more about us on our website and be sure to check out our laboratory section to explore the fantastic infrastructure that SWITCH has to offer!


The Jobs

Together with the PIs of the Switch Lab you will be part of a team of post docs and technicians and will be a driving force for this project. You will be well supported on an administrative level, allowing you to focus on the science, both hands-on in the lab and analyzing data.

Position 1 – Cellular biology of heterotypic amyloid interactions

  • PhD in a topic related to protein aggregation or protein homeostasis
  • Expertise in cellular biology of protein aggregation and related assays
  • Strong interest in protein aggregation and its role in disease.
  • A solid publication record with first-author research publication(s) in peer-reviewed international journals
  • Highly motivated, enthusiastic, critical and creative
  • Written and oral communication skills of the highest level
  • The ability to work in a multidisciplinary team
  • Prior supervisory or project coordination experience is a plus

Position 2 - Biophysics of heterotypic amyloid interactions

  • PhD in a topic related to protein aggregation /protein biophysics
  • Expertise in biophysical or biochemical methods to study protein aggregation
  • Strong interest in protein aggregation and its role in disease.
  • A solid publication record with first-author research publication(s) in peer-reviewed international journals
  • Highly motivated, enthusiastic, critical and creative
  • Written and oral communication skills of the highest level
  • The ability to work in a multidisciplinary team
  • Prior supervisory or project coordination experience is a plus

We offer
  • A vibrant, world-class research environment operating at an international level
  • Access to the resources of two host institutions:
    • VIB , an excellence-based research institute
    • KU Leuven, one of Europe’s leading research universities
  • State-of-the-art research facilities . 
  • A dedicated training program  to broaden your expertise and enhance your skill set.
    At SWITCH we pay particular attention to the career development goals of our people and actively support the ambitions of our lab members in the lab and beyond. Information on SWITCH Lab alumni can be found here .
  • A competitive compensation package based on expertise and experience

Starting Date: as soon as possible


How to apply?

For more information contact  [email protected]. Please complete the online application procedure and include a detailed CV including list of publications, a motivation letter, and the contact information of at least two referees.



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