Newswise — A research team at the University of Montreal’s Department of Chemistry has just developed a new tool to study the encounter between members of two families of biomolecules essential to life: sugars and proteins. This work, which paves the way for many applications, has recently been Angewante Chemie a famous scientific journal in chemistry.
Biologically ubiquitous sugars
“Caramel, candy, chocolate”…sugar is omnipresent in our lives, but not just in the sense that most people understand. In fact, in the large biological family, carbohydrates extend far beyond our dietary enjoyment and include a huge variety of natural biomolecules.
“Every cell that makes up our world is coated with sugars, and this is true for all living things. These carbohydrates are therefore at the forefront of almost every biological process, and are essential to our It plays a fundamental role in maintaining the body’s health and in causing certain diseases,” argues Sammy Cecioni, professor in the Department of Chemistry at UdeM.
He continues: “Scientists have long thought that these complex sugars were simple decorations on cells. We now know that sugars are linked to many other molecules, especially lectins, a large family of proteins. We know we’re interacting.”
Sugar, lectin, bacteria, virus, cancer cells
Lectins, also called “hemagglutinins,” are natural proteins that exist in all living organisms and have the unique ability to recognize sugars and temporarily bind to them.
This specific and reversible carbohydrate recognition is involved in a variety of biological processes, including cell-to-cell recognition in the immune response triggered by infection.
Lectin research is a rapidly growing field. Scientists have discovered that lectins “stick” to sugars…and that this binding is involved in the development of many diseases.
“The more we study this phenomenon between sugars and lectins, the more we realize its essential importance in biology. From influenza viruses that attach to our cells and cause infections, to cancer cells that trick our immune systems to avoid being destroyed, we know that each time a story of encounter is born. “Between lectins and sugars,” summarizes Sammy Cecioni.
Sugar and lectins: a stealthy, low-intensity encounter
However, it is not easy to detect when sugars bind to some of these lectins, so some pieces are missing from the puzzle to understand how binding occurs.
These interactions are generally covert and low intensity. Cecil Bouche, a master’s student in Professor Cecioni’s lab, and his doctoral colleague Brandon Wurz came up with the idea of using light to illuminate these interactions. Together with the professor, they created a type of chemical probe that can irreversibly “freeze” the interaction between sugars and lectins, causing them to fluoresce.
The key-lock model image is often used in general science to explain how biomolecules interact. To be able to study this biochemical encounter, chemists have already engineered molecules that can form new chemical bonds that block the lock (lectin) from the lock (sugar) and determine which sugars are good for health. We were discovering whether it binds to important lectins.
Professor Cecioni’s team’s idea was to attach a reactive chromophore (a group of atoms that gives a molecule its color) to sugars, allowing them to activate the “key” function of fluorescence when bound to lectins. Ta. When proteins are captured and emit fluorescence, it becomes much easier for scientists to study the underlying mechanisms and their destruction.
Professor Cecioni and his students are confident that the technique they have developed can be used with other types of molecules. You can also control the color of new response keys that are created. By allowing visualization of interactions between molecules, this discovery expands the collection of tools for the study of biological interactions and has the potential to color the very incomplete vision of sugar recognition. .
About this study
article ” Fluorescence photocrosslinking of glycan-binding protein recognition using fluorinated azide-coumarin fucosides ” was published on October 17, 2023 by Cécile Bousch et al. Angewante Chemie.
This research was funded by the Natural Sciences and Engineering Research Council of Canada, the Quebec Natural Sciences Foundation, and the Canadian Foundation for Innovation.
About Professor Sammy Cecioni
2019 Department of Chemistry recruitment, Sammy Cecioni is a young researcher specializing in the emerging fields of biochemistry and glycomics. He received his first of the 2021 Research Excellence Medals from UdeM’s Faculty of Arts and Sciences.
“Our research team is developing new tools to accelerate discoveries in the field of glycoscience. A series of molecules modified by sugars can be described as the ‘dark matter’ of life.” “We propose an interdisciplinary approach at the intersection of chemistry and biology to enable advances relevant to human health,” he says. Want to know more? listen Professor Cecioni will discuss the research conducted in his lab.