Using galectin-10 protein crystals, researchers have taken great steps in elucidating the molecular structure of sugars. This exciting new research, published in last month’s issue of the journal Small Structures, demonstrates how these unique crystals can capture and study sugar molecules. Combined, these discoveries have tremendous potential to accelerate advances in glycobiology, drug discovery and biomaterials.
The research team, headed by Mariko Kojima, used a cell-free crystallization method to grow galectin-10 protein crystals suitable for X-ray analysis. To further refine the creation process, the engineers soaked these specially engineered crystals in a sugar solution. In less than a day, the crystals recorded all of their atomic details for five different sugars. Notably, the researchers replaced a single amino acid (E33A) in the galectin-10 protein, enabling sugar molecules to fit more snugly within the crystal framework.
This thee amendment a counterbalancing effect while helping up positively transform the study’s impact. It illustrated how even small alterations to protein structures can have huge effects on sugar binding. To further demonstrate these crystals, the research team presented their remarkable rapid structure determination capabilities. Their work led to the first atomic-resolution image of melezitose, a complex sugar that defied high-resolution imaging until it was shiny enough to hold its form.
“We developed scaffold-like crystals of Gal-10 that hold sugar molecules within their network, allowing us to visualize the precise conformations of sugars at the atomic level using X-ray techniques,” – Takafumi Ueno
The new capability to visualize sugars quickly expands new avenues for exploration. Here’s how scientists used super-resolution imaging to track sugar molecules and understand their interactions with proteins. This advanced capability is now essential for elucidating much of the biological underpinnings.
“Being able to visualize these sugars so rapidly gives us an entirely new way to explore their behavior,” – Takafumi Ueno
Galectin-10 protein crystals have been very successful at elucidating complex sugar arrangements. The process provides the basis for rapid screening of hundreds of sugars and small molecules. This would open the door to quicker breakthroughs across many disciplines.
“With our system, researchers could screen hundreds of sugars and small molecules within a short time span, accelerating discoveries in glycobiology, drug development and biomaterials,” – Takafumi Ueno
The implications from this research are to reinforce our existing understanding that sugars, or saccharides, have roles that go well beyond just sweetening food. Unlocking their molecular structures is key to unlocking radical advances across health and science.