• 11/6/2025
  • Reading time 2 min.

European funding for outstanding research into biotechnology at TUM

ERC Synergy Grant for Prof. Johannes Buchner

Alzheimer's, Parkinson's, and certain types of cancer – many serious diseases arise when misfolded proteins cause malfunctions in the body. An international research team now wants to decipher the role of “helper proteins” called chaperones, which are responsible for quality control of newly produced proteins in the body. To this end, the CHAPEROME project is receiving funding of almost €11 million through a Synergy Grant from the European Research Council (ERC).

Prof. Johannes Buchner Andreas Heddergott / TUM
Teaming up with researchers from Göttingen and Stanford, Prof. Johannes Buchner will investigate chaperones, proteins that are responsible for quality control in cells. This research is funded by the European Research Council with an ERC Synergy Grant.

Scientists at TUM have so far been able to secure a total of 255 ERC grants. These now include six Synergy Grants from the highest funding category. The total amount for CHAPEROME is almost €11 million, of which over €3.2 million is allocated for the Technical University of Munich (TUM). Synergy Grants are always awarded to teams of researchers with equal status. The CHAPEROME team consists of Prof. Marina Rodnina from the Max Planck Institute for Multidisciplinary Sciences in Göttingen, Prof. Johannes Buchner from the TUM, and Prof. Judith Frydman from the Stanford University in the USA.

The CHAPEROME research project

Proteins are among the central building blocks of life. Without them, cells and organs could not function. Proteins are long chains of amino acids that are assembled in every cell by large molecular machines called ribosomes. Depending on the amino acid sequence, these chains fold into a specific three-dimensional structure. This structure determines whether a protein can perform its desired function.

Misfolded proteins cause a variety of serious neurodegenerative diseases, prion diseases such as Creutzfeldt-Jakob disease or BSE, but also metabolic and hereditary diseases such as cystic fibrosis and phenylketonuria. Some types of cancer also develop or worsen when proteins that regulate cell growth are misfolded.

Chaperones are active in cells to prevent such malfunctions. Among other things, they support the correct folding of proteins and can repair incorrectly folded molecules. New findings by the CHAPEROME team suggest that chaperones also regulate how ribosomes produce proteins. Over the next six years, the funded team aims to work together to find out how this works at the molecular level.

In addition to discovering fundamental mechanisms, e.g., in the formation of nerve cells, the project could also provide new approaches for treating diseases caused by protein folding disorders in the long term.

Further information and links
  • The project name CHAPEROME draws a parallel to terms such as proteome, which refers to the entirety of proteins.
  • The name “chaperone” originally comes from French and means “companion” or “escort.”
  • European Research Council (ERC)

Technical University of Munich

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