Prof. dr hab. Krzysztof Liberek, from IFB UG and MUG, has been awarded the Foundation for Polish Science 2023 Prize in the area of Life and Earth Sciences for demonstrating the role of chaperone proteins in the recovery of proteins from aggregates and their folding into an active form. The so-called ‘Polish Nobel Prize’ is awarded for exceptional scientific achievements and discoveries that push the boundaries of cognition and open new cognitive perspectives, make an outstanding contribution to the civilisational and cultural progress of our country, and ensure Poland's prominent place in tackling the most ambitious challenges of the modern world.

The awards were granted by the Foundation for Polish Science for the 32nd time.

‘The Foundation's award is a great and unique honour for me. In modern experimental science, discoveries result from a whole research team’s work. I would like to thank the members of my team for their contribution to the award-winning results. I am all the more pleased with the Foundation Award as the Foundation promotes the quality of the research conducted and not the number of published papers,' said prof. Krzysztof Liberek.

In 2023, the FPS Prize was awarded to four outstanding scientists: prof. Krzysztof Liberek, prof. Rafał Latała, prof. Maria Lewicka and prof. Marcin Stępień.

The Prize of the Foundation for Polish Science is an individual distinction awarded by the Foundation Council through a contest. Laureates are selected from among candidates submitted by outstanding representatives of the scientific community, invited by name by the Council and the FPS Board. The FPS Council acts as the Jury of the competition. It selects the laureates based on the opinions of independent experts and reviewers - mainly from abroad - evaluating the candidates' achievements. The prize is awarded in four areas: Life and Earth Sciences, Chemical and Material Sciences, Mathematical and Physical Sciences and Engineering, and Humanities and Social Sciences.

Prof. Krzysztof Liberek is a pioneer in molecular research on chaperone proteins. He received the Foundation for Polish Science 2023 Award for demonstrating the role of chaperone proteins in recovering proteins from aggregates and folding them into an active form.

Chaperone proteins are synthesised in the cells of all known organisms. Their amino acid sequences are evolutionarily conserved, demonstrating the importance of their function for the cell. They are proteins that, among other things, are responsible for the correct folding of other proteins, both under physiological and stress conditions. This gives the proteins their proper spatial structure, essential for performing their tasks in the cell. Chaperone proteins participate in the construction of protein complexes without being part of their final active structure (hence their name), and they also prevent the aggregation of other proteins and participate in the recovery of active proteins from protein aggregates. This is a crucial function, as aggregated proteins can be toxic to the cell. Much evidence suggests that such protein aggregates are present in some neurodegenerative diseases (e.g. Alzheimer's disease). Some of these aggregates may be solubilised in the cell with the involvement of chaperone proteins.

Understanding the mechanisms of action of chaperone proteins is very important for practical purposes - in medicine, pharmacology and biotechnology. In simple terms, the role of chaperone proteins is to control the quality of the state of other proteins. When, due to a change in the amino acid sequence or external conditions, proteins become abnormally folded (do not adopt the correct spatial structure), chaperone proteins unfold the 'defective' protein and allow it to fold back properly. Other types of chaperone proteins may be involved in the folding process. If this 'repair' reaction does not occur and the protein is still badly folded, the chaperone proteins stimulate the degradation of these abnormal proteins. They thus do their best to ensure that misfolded proteins do not accumulate in the cell, thus preventing the formation of protein aggregates, which can lead to pathological conditions. By taking care of the state of other proteins in this way, chaperone proteins play an essential role in protecting cells and whole organisms from adverse environmental conditions.

Using new research techniques from biochemistry and biophysics, prof. Krzysztof Liberek has demonstrated in a series of five papers published between 2016 and 2021 and awarded the FPS Prize the complexity of the process by which chaperone proteins lead to the recovery of proteins from protein aggregates and their folding into an active spatial structure. He showed 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 chaperone proteins to disaggregate them afterwards effectively. If protein aggregation occurs in the presence of sHsp, at the first step of the disaggregation process, chaperone proteins (belonging to the Hsp70 family) remove sHsp from the surface of the aggregate, simultaneously initiating the unfolding of the proteins that make up the aggregate. The partially unfolded proteins undergo, with the cooperation of other chaperone proteins belonging to the Hsp100 family, complete unfolding and release from the aggregate. This allows the proteins to fold into the correct structure, which no longer interacts with the rest of the aggregate. Repeating this process multiple times leads to complete dissolution of the aggregate and recovery of the pool of active proteins.  While still working on his PhD, Krzysztof Liberek discovered that proteins belonging to the Hsp70 family interact with accessory chaperone proteins belonging to the SPD family. In a series of papers that formed the basis for the FPS Prize, prof. Liberek showed, by monitoring the aggregate dissolution process in real-time, that class B SPD proteins promote the binding of Hsp70 proteins to aggregates, which stimulates the disaggregation process. The activity of class A SPD proteins, on the other hand, is vital in protecting proteins from aggregation and in the process of their folding to the native structure. This discovery explains the phenomenon observed for many years by molecular biologists that, depending on the SPD proteins, the Hsp70 family proteins can have different functions.

Prof. Krzysztof Liberek's discoveries on the mechanisms of action of chaperone proteins 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 an increasing number of people worldwide (in Poland, it is already more than 350,000 people) and poses a huge medical, social, and economic challenge.

The FPS Prizes have been awarded since 1992. The group of laureates, including this year's winners, already comprises 117 people. Among them are eminent scholars and scientists, such as Tomasz Dietl, Marcin Drąg, Elżbieta Frąckowiak, Lech Gradoń, Ryszard Horodecki, Leszek Kaczmarek, Zofia Kielan-Jaworowska, Maciej Lewenstein, Krzysztof Matyjaszewski, Karol Modzelewski, Karol Myśliwiec, Bohdan Paczyński, Marek Samoć, Jan Strelau, Timothy Snyder, Jerzy Szacki, Andrzej Szczeklik Andrzej K. Tarkowski, Andrzej Trautman, Anna Wierzbicka.

The award ceremony will take place on December 6 this year and will be broadcast online.

In the current term, the Council consists of Professors:

- Tomasz Guzik (Collegium Medicum of the Jagiellonian University) - Chairman of the Council,

- Grażyna Jurkowlaniec (Institute of Art History, Faculty of Arts and Culture Sciences, University of Warsaw) - Vice-chair of the Council,

- Piotr Garstecki (Institute of Physical Chemistry, Polish Academy of Sciences, Warsaw),

- Jan Kotwica (Institute of Animal Reproduction and Food Research, Polish Academy of Sciences, Olsztyn),

- Tomasz Łuczak (Faculty of Mathematics and Computer Science, A. Mickiewicz University in Poznań)

- Aleksandra Łuszczyńska (SWPS University),

- Maria Nowakowska (Department of Chemistry, Jagiellonian University).

The amount of the award is PLN 200 000.

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The Foundation for Polish Science has existed since 1991 and is an independent, self-financing, non-profit, non-governmental institution that pursues the mission of supporting science. It is the largest non-budgetary source of science funding in Poland. The statutory objectives of the FPS include supporting outstanding scientists and research teams and working towards transferring scientific achievements into economic practice. The Foundation pursues them by awarding individual prizes and scholarships for scientists, granting subsidies for implementing scientific achievements into economic practice and supporting important undertakings serving science (such as publishing programmes or conferences). The Foundation is also committed to supporting international scientific cooperation and increasing the scientific independence of the younger generation of scientists.

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Prof. dr hab. Krzysztof Liberek - biogram

Krzysztof Liberek was born in 1958 in Gdańsk. He completed his Master's in physics at the Gdańsk University of Technology (1982) and obtained his PhD in molecular biology and habilitation in biological sciences at the University of Gdańsk (1990 and 1996 respectively). He completed a postdoctoral fellowship at Utah State University, USA, in 1990-1991 and another in 1992-1993 at the University of Geneva, Switzerland. He was awarded the academic title of professor in 2002. In 2006, he became a member of EMBO (an organisation of leading scientists and promoting excellence in life sciences in Europe and worldwide). He is a laureate of many scientific awards - among others, he received three times the Award of the Minister of Education and Higher Education, three times the Award of the Rector of the University of Gdańsk (for the best publication) and the Scientific Award of the Mayor of the City of Sopot (of which he is a long-term resident). Winner of several grants from the Committee for Scientific Research, the Ministry of Education and Higher Education and the National Science Centre (including the Maestro grant in 2013), as well as the TEAM programme of the Foundation for Polish Science (in 2009); several times member of the panel evaluating European Research Council (ERC) grants; reviewer in renowned scientific journals in the field of molecular biology.

Prof. Krzysztof Liberek can also be proud of his success in educating young scientists: he is the supervisor of 17 defended doctoral theses; four of his students received the START scholarship from the Foundation for Polish Science, and two received the Prime Minister's Award for the best doctoral dissertation. He currently heads the Department of Protein Biochemistry at the Intercollegiate Faculty of Biotechnology UG and MUG. His research interests are in the structure and mechanisms of action of chaperone proteins in various cellular processes. In particular, he is working on determining the molecular mechanism of cooperation between chaperone proteins involved in recovering active proteins from protein aggregates.