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The day has finally arrived. Scientists eventually created synthetic mucus molecules that exhibit the structure and function of the real deal.
Far from being a slimy crime, however, it’s a discovery that could help scientists design new treatments for infectious diseases, according to the research team behind the breakthrough.
Slippery, slimy, and oozing, the mucus looks pretty disgusting. However, as unpleasant as we may find it, the trick is biologically useful: it acts as a barrier protecting and hydrating delicate tissues, trapping microbes (for which it is also loaded with antimicrobial enzymes) and contaminants, and aiding the body to expel them.
Our body produces between 1.5 and 2 liters (1.5 to 2 pints) of mucus each day in the airways alone; it covers our airways, lungs and gastrointestinal tract – we are practically miracle glue sacks.
If we could replicate its properties, it could provide us with an important tool in the fight against disease, and this new research is an important step. Scientists led by MIT chemist Austin Kruger synthesized mucins, the building blocks of mucus proteins.
Mucins are made up of a long protein spine bristling with strands of carbohydrate polymers called glycans (much like a fuzzy pipe cleaner); it is not known how polymers contribute to the various properties of mucus. Previous research has shown that they interfere with the ability of bacteria to communicate with each other, attach to surfaces, and secrete toxins.
The team’s synthetic mucins, built around a polymer backbone, might help figure this out – not only are they structured like the real thing, but they even mimic some of its functions.
“We would really like to understand what characteristics of mucins are important for their activities and mimic those characteristics so that you can block virulence pathways in microbes,” said MIT chemist Laura Kiessling.
The difficulty is that the mucins are complicated. The protein backbone is made up of thousands of different amino acids, scientists said, and there are many different types of glycans that can make up body hair.
The team started with carbon ring molecules and used a process that opened them in a straight line. The resulting molecules, each containing a carbon-carbon double bond, were then joined to form the polymeric spine of synthetic mucin.
Each carbon atom in the bond is usually bonded to a different chemical group, and the polymer can take different shapes depending on where they are attached. In cis form, both groups – carbon and the other, whatever it is – are on the same side; in the trans form, they are on opposite sides.
The team created both forms in their attempt to synthesize mucins and put them to the test.
The trans polymers turned into weird little drops that didn’t look much like mucins. They were also not particularly effective at capturing toxins secreted by the Vibrio cholerae bacterium.
However, the cis polymers remained elongated; and, when exposed to V. cholerae, not only did they capture toxins efficiently, but they were even better than real mucins.
There is still a lot to do – the team’s work did not include the glycan hairs – but this is already showing great promise. The team has perfectly demonstrated that the elongated shape of the spine plays an important role in the functioning of mucins.
Additionally, the team found that the cis polymers were soluble in water – more than natural mucin – meaning they have potential for inclusion in topical creams and gels, and possibly even eye drops.
“Our results,” they wrote in their paper, “describe a critical design principle for synthetic mucin mimics that will guide future studies on the role of mucin in microbial symbiosis and pathogenesis and serve as a model for generate mucin mimics that act as lubricants or control the microbiome. composition and infectious disease. “
The research was published in ACS Central Science.
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