PhD position in the field of rare amyloidosis diseases

Updated: about 2 months ago

Topic

Amyloidosis disease is the abnormal accumulation of protein in amyloid conformation in vital organs and tissues throughout the body, ultimately resulting in multiorgan dysfunction, organ failure and a lethal outcome if left untreated. A major difficulty for proper diagnosis is to correctly identify the type of amyloid accumulating in a particular patient.

We are establishing Belgium’s first amyloidosis expertise center “BE-Amycon”, funded by a VIB Grand Challenges grant and in collaboration with researchers from UGent, and clinicians at UZ Leuven and UZ Gent. This large multi-disciplinary initiative aims to have a high societal impact by delivering improved diagnostics methods, supporting patient care and developing new disease treatments. To deliver in this ambitious challenge we are looking for a highly motivated PhD student to join our amyloidosis research team at the Switch lab.

A key to generating new diagnostics, biomarkers and treatments is to understand the interactions that accumulating amyloid establishes in the affected organs. The candidate will be directly supervised by an experienced amyloid scientist and, in direct collaboration with partners at VIB proteomics facility and UZGent, will work towards implementing Mass Spectrometry (MS) proteomics-based methods to accurately identify the amyloid-type, to perform biomarker discovery and to identify interaction partners We will confirm these interactions by in situ cryogenic tomography to visualise and determine the contribution of these interactions in the pathology of the affected organs.

The candidate will also be co-supervised by clinicians Professor Michel Delforge and Professor Koen Poesen, which offers a unique opportunity to experience both basic and clinical aspects of biomedical research. This journey brings together different fields of science, so the candidate is expected to have a keen interest in finding, mastering and applying cutting-edge technologies to solve this challenge. Curious to find out more? Read below to find out how to apply! 


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!


What we are looking for

Essential

  • You hold an M.Sc. or M.D. degree, with minimally distinction grades or higher
  • You meet the English language criteria of KU Leuven
  • You have a strong interest in (the physics of) protein structure and its relation to biology
  • Highly motivated, enthusiastic, critical and creative
  • The ability to work in, and communicate fluently with a multidisciplinary team is a must

Desirable but not required

  • Prior experience with any of the core themes, i.e. protein biophysics or protein biochemistry, mass spectrometry, cryogenic-electron microscopy/tomography is considered a plus
  • You are willing to work with patient tissue and animal models (Felasa B certificate is a plus)

We offer
  • A versatile and challenging job
  • 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 skillset

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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