Faster Method to Identify Proteins Based on Amino Acid Content Developed

Researchers at the University of Gothenburg have devised a novel method to identify proteins by analyzing their amino acid content, rather than relying on their structure. This approach offers a faster, easier, and more reliable alternative to existing methods. While the prevailing belief is that a protein's structure dictates its function, many proteins lack well-defined structures.

Lead researcher Gergely Katona developed a scanning method that examines proteins based on the number of amino acids they contain, enabling the identification of proteins and their functions. Through this approach, the researchers successfully predicted the amino acid combination required to bind to the protein survivin, achieving a reliability of approximately 80%, surpassing the identification accuracy obtained through the use of protein structures. The findings were published in iScience.

The study revealed that the amino acid content of peptides, rather than their structure, significantly influenced their binding to survivin. Katona emphasizes that counting the number of amino acids has proven successful in science and yielded surprisingly accurate predictions of protein function.

The researchers highlight the advantages of this protein scanning method, particularly in combination with machine learning (AI), which accelerates the process of linking amino acid types and numbers to specific functions. This advancement holds the potential to expedite the development of new biological drugs.

Furthermore, the scanning method led to the discovery of a previously unknown function of the protein survivin. Although survivin primarily prevents programmed cell death in embryo cells, it becomes deregulated in cancerous tumors, contributing to cancer development. The study found that survivin directly influences another protein called PRC2, responsible for regulating various functions in cell DNA. Dysfunctional PRC2 is associated with different types of cancer. Current cancer drugs target both survivin and PRC2, but the newfound link between the two proteins suggests that drug designs may need to be modified to avoid potential side effects.

By suppressing survivin levels, the researchers observed an increase in PRC2 activity. Identifying the precise targets in the atomic sequences to balance survivin and PRC2 holds promise for pharmaceutical companies in designing more effective cancer treatments.