In a groundbreaking discovery, scientists have identified the first natural fractal molecule, a microbial enzyme called citrate synthase from a cyanobacterium, which assembles into a Sierpiński triangle pattern. This finding, led by researchers from the Max Planck Institute and Philipps University in Marburg, marks the first instance of a regular molecular fractal observed in nature. Unlike other molecular structures that lose their pattern at larger scales, this fractal maintains self-similarity across different scales, challenging previous understandings of molecular assembly.
The discovery was made using electron microscopy, revealing the enzyme’s unique ability to form triangular patterns that maintain their shape regardless of size. This fractal formation results from asymmetrical interactions between protein chains, deviating from the symmetrical patterns seen in other self-assembling proteins. Interestingly, when researchers genetically modified the cyanobacterium to prevent fractal assembly, it showed no impact on the organism’s growth, suggesting the fractal formation might be an evolutionary accident without a specific functional purpose.
This unexpected discovery not only adds a new dimension to our understanding of molecular structures but also hints at the potential for more complex and undiscovered molecular assemblies in nature. It challenges scientists to rethink the rules of molecular self-assembly and opens up new avenues for exploring the evolutionary pathways that lead to such intricate structures.
Read more…