Professor Krzysztof Liberek from the Intercollegiate Faculty of Biotechnology of the University of Gdańsk and the Medical University of Gdańsk received the 2023 FNP Prize in the field of life sciences for demonstrating the role of chaperone proteins in recovering proteins from aggregates and folding them into the active form.

Professor Krzysztof Liberek was born in 1958 in Gdańsk. He graduated with a Master’s degree in physics from the Gdańsk University of Technology in 1982, obtained his doctorate in molecular biology in 1990, and habilitation in biological sciences at the University of Gdańsk in 1996. He completed a postdoctoral fellowship at the University of Utah, USA, in 1990–1991, and another one in 1992–1993 at the University of Geneva, Switzerland. He received full professorship in 2002. In 2006, Liberek became a member of the European Molecular Biology Organization – an organization of leading scientists that promotes excellence in life sciences in Europe and around the world. He is a recipient of many science awards: the Award of the Minister of Education and Science (three times), the Award of the Rector of the University of Gdańsk (three times; for the best publication), and the Science Award of the Mayor of the City of Sopot, of which he is a long-term resident. He is the laureate of several grants from the Committee for Scientific Research, the Ministry of Education and Science, and the National Science Centre (including the Maestro grant in 2013), and the TEAM programme of the Foundation for Polish Science (in 2009). Several times, he was a member of the panel evaluating European Research Council (ERC) grants and a reviewer in renowned scientific journals in the field of molecular biology.

Moreover, Professor Krzysztof Liberek successfully trains early career scientists. He was the supervisor of seventeen completed doctoral theses, four of his students received the START stipend from the Foundation for Polish Science, and two of them received the Prime Minister’s Award for the best doctoral thesis. He is currently the Head of the Laboratory of Protein Biochemistry at the Intercollegiate Faculty of Biotechnology. His research interests focus on the structure and mechanisms of action of chaperone proteins in various cellular processes. In particular, he seeks to determine the molecular mechanism of cooperation between chaperone proteins involved in the recovery of active proteins from protein aggregates.

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Professor Krzysztof Liberek is a pioneer in the field of molecular research on chaperone proteins. He received the 2023 FNP Prize in the field of life sciences for demonstrating the role of chaperone proteins in recovering proteins from aggregates and folding them into the active form.

The name chaperones refers to proteins that participate in the formation of protein complexes without being part of their final active structure. Chaperone proteins are synthesized in the cells of all known organisms. Their amino acid sequences are evolutionarily conserved, demonstrating the importance of their function for the cell. Among other functions, these proteins are responsible for the errorless folding of other proteins, both under physiological and stress conditions. This gives proteins their correct structure, which is essential for them to perform their tasks in the cell. Furthermore, they prevent the aggregation of proteins and are involved in the recovery of active proteins from protein aggregates. This is an important function, as aggregated proteins can be toxic to cells. Evidence suggests that such protein aggregates are present in some neurodegenerative diseases like the Alzheimer’s disease. Some of these aggregates can be dissolved in the cell with the involvement of chaperones.

Understanding the mechanical basis of chaperones’ function is very important for practical purposes in medicine, pharmacology, and biotechnology. In simplified terms, chaperone proteins conduct quality assessment of the state of other proteins. When proteins misfold due to external conditions or a change in the amino acid sequence (failing to adopt the correct structure), chaperones unfold the ‘defective’ protein, allowing it to fold back into the correct structure. Other types of chaperones may be involved in the folding process. If this ‘repair’ reaction does not occur and the protein remains misfolded, chaperones stimulate the degradation of these abnormal proteins. Therefore, chaperones ensure that misfolded proteins do not accumulate in cells, thus preventing the formation of protein aggregates that could lead to pathological conditions. Such attention to the fitness of other proteins means that chaperones play essential roles in protecting cells and whole organisms from adverse environmental conditions.

Using new research techniques in biochemistry and biophysics, Liberek demonstrated in a series of five articles published between 2016 and 2021 – for which he received the FNP Prize – the complexity of the process by which chaperone proteins engender the recovery of proteins from aggregates and their folding into an active structure. Liberek has shown that the presence of small heat shock proteins (sHsps) during protein aggregation significantly alters the structure of the resulting protein aggregates, making it easier for other chaperones to effectively disaggregate them. If protein aggregation occurs in the presence of sHsp, then in the first step of the disaggregation process, chaperones belonging to the Hsp70 family remove sHsps from the surface of the aggregate, simultaneously initiating the unfolding of the proteins trapped in the aggregate. With the cooperation of other chaperones belonging to the Hsp100 family, the partially unfolded proteins undergo a complete unfolding and release from the aggregate. This allows the proteins to fold into the correct structure. Repeating this process multiple times leads to the complete dissolution of the aggregate and the recovery of active proteins. While still working on his doctorate, Liberek discovered that proteins belonging to the Hsp70 family interact with auxiliary chaperone proteins belonging to the JDP family. In a series of articles, for which he received the FNP Prize, Liberek demonstrated aggregate dissolution in real time and showed that class B JDP proteins promote the binding of Hsp70 proteins to aggregates, which stimulates the disaggregation process. On the other hand, the activity of class A JDP proteins is important in protecting proteins from aggregation and in the process of their folding to the native structure. This finding explains the phenomenon observed for many years by molecular biologists, namely that depending on the JPD proteins, the Hsp70 family proteins can fulfill different functions.

Professor Krzysztof Liberek’s discoveries on chaperone proteins may have important biomedical implications. Among other things, they may contribute to the understanding of the molecular mechanisms underlying neurodegenerative disorders, such as Alzheimer’s disease, which affects a growing number of people worldwide and poses a huge medical, social, and economic challenge. Suffice it to mention that in Poland already more than 350,000 people struggle with Alzheimer’s.

 

Fot. Magdalena Wiśniewska-Krasińska

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