The illustration shows how different areas of PRC2 protein (the one on the right side) binds to survivin. The researchers chopped the PRC2 sequence into units of 15 amino acids and arranged them on a grid. Each pixel in that grid is 1 unit. The colour shows binding strength to survivin. Blue means the unit in that pixel doesn't bind/binds weakly to survivin, and the bright pink pixels are the strongest binders.
Newswise — Scientists at the University of Gothenburg have made a groundbreaking breakthrough by devising a method to detect proteins in living cells without relying on their structural characteristics. This innovative approach surpasses previous techniques in terms of speed, simplicity, and accuracy.
The prevailing notion suggests that the function of proteins within cells is primarily governed by their structural attributes. The arrangement of atoms in a protein, known as its atomic sequence, determines its overall structure and shape. However, it is worth noting that numerous proteins do not possess a clearly defined structure.
A novel approach has been pioneered by scientist Gergely Katona, which involves scanning proteins to determine their identity and function based on the count of amino acids or different atoms they possess, rather than relying on their structural characteristics. Through this scanning technique, the research team achieved a significant advancement by accurately predicting the specific combination of amino acids required to bind to the protein survivin. Remarkably, this method demonstrated a reliability of approximately 80 percent, surpassing the effectiveness of utilizing the protein's primary structures for identification. The findings of this study have been recently published in the esteemed scientific journal iScience.
The structure of less importance
The researchers conducted extensive experiments involving several thousand peptides, each consisting of 15 amino acids. Remarkably, their findings led them to conclude that the binding of these peptides to survivin was primarily influenced by the composition of amino acids, rather than the structural characteristics of the peptides. The researchers discovered that the specific amino acid content played a crucial role in determining the binding affinity with survivin, while the structural aspects of the peptides had minimal significance in this context. This discovery highlights the significance of amino acid composition in understanding the binding mechanisms of peptides to survivin.
Gergely Katona emphasizes the effectiveness of a simple counting approach in scientific research, stating that it has frequently yielded successful results. In this particular study, the researchers employed a counting method by quantifying the number of amino acids present in proteins, enabling them to remarkably predict the protein's function. This approach proved to be highly effective, highlighting the significant role played by amino acid count in determining protein functionality. Gergely Katona's statement underscores the power of a straightforward yet insightful methodology in scientific investigations.
The scientists perceive benefits with this protein-scanning technique. Artificial intelligence (AI) similarly expedites the correlation between amino acid quantity and category to a specific function. Consequently, the advancement of novel biological medications can be hastened.
During the researchers' trials with this fresh scanning approach, an entirely novel role of the survivin protein was additionally unveiled. Primarily prevalent in embryonic cells, this protein impedes programmed cell death. However, in cancerous tumors, survivin undergoes dysregulation, thereby promoting cancer progression.
Useful in cancer research
The researchers have recently observed a direct correlation between survivin and another protein called PRC2, which acts as a regulator, turning specific functions on and off within the cell's DNA, similar to programming. Dysfunctional PRC2 has also been associated with different types of cancer. Current cancer medications aim at targeting both survivin and PRC2. However, given the newly uncovered connection between survivin and PRC2, the design of these drugs may need to be modified to prevent severe side effects.
"We observed that reducing the expression of survivin led to an increase in PRC2 activity," explains Gergely Katona. "The ultimate goal for pharmaceutical companies is to identify the precise targets within the atomic sequences that would enable us to achieve a delicate balance between these two proteins."
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