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Tree diagram showing genetic similarity between 71 proteins versus 180 associated proteins previously found in other molluscs. The results confirm that even when compared to hundreds of other proteins at once, similar proteins still cluster together. The black bracket on the right indicates the ‘outgroup’, which is a group of proteins that are intentionally unrelated to the rest. Credit: Antonio Cirullo

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Tree diagram showing genetic similarity between 71 proteins versus 180 associated proteins previously found in other molluscs. The results confirm that even when compared to hundreds of other proteins at once, similar proteins still cluster together. The black bracket on the right indicates the ‘outgroup’, which is a group of proteins that are intentionally unrelated to the rest. Credit: Antonio Cirullo

What is snail mucus? That’s the question researchers asked in a new study looking at the molecular makeup of snail mucus. When analyzing the mucus of common garden snails, they found that it contained a complex set of proteins, some of which were identified as completely new.

In a newly published paper in Nature Communications, scientists describe the mucus of Corno aspericum—a species used in cosmetic products and eaten like snails—and detail the composition of three unique types of secretion—one that moisturizes and protects its skin, and one that acts as a glue-like adhesive. and another that lubricates to allow the animal to move freely across surfaces.

“We were surprised that the compositions of the mucus were so different, even though they were produced from the same species,” said lead author Antonio Cirullo, PhD, a biochemist. Student at the Graduate Center of the City University of New York. “More than that, the sticky snail’s glue and the snail’s gliding track, which have diametrically opposite purposes, come from the same part of the snail. It was exciting to discover that very subtle differences in the compositions of the mucus have enormous effects on their biology and material properties.”

The researchers say the hydrogels contain ions, sugars and more than 70 proteins, including enzymes, myosins, lectins and matrix proteins. About a third of the proteins found in the mucus did not match any proteins in the global databases searched, the researchers said. In short, secretions contain many proteins unlike any other known to science.

Snail mucus is widely used in cosmetics, moisturizers, anti-aging creams, wound care treatments, and antimicrobials. Snail mucus-infused beauty products are a multi-billion dollar global industry.

There are still many open questions about the molecular makeup of mucus. Even human mucus, which has been studied much more extensively than snail mucus, is not well understood.

“Everyone is fascinated and disgusted with mucus,” said lead study author Adam Braunschweig, a faculty member of the Nanoscience Initiative at the Center for Advanced Science Research. “However, most people don’t realize how complex and elegant these secretions are.” at the City University of New York Graduate Center (CUNY ASRC) and Professor of Chemistry and Biochemistry at the Graduate Center and Hunter College.

The data revealed small differences that accounted for large differences in mucus properties. One example involves the use of calcium.

Calcium binds mucus networks together and strengthens the network. As a result, lubricating mucus contains the lowest amount of calcium and the highest amount of calcium-binding proteins, while bound mucus has the opposite composition.

Snail mucus is currently being studied for its biomedical applications, including in surgical adhesives, as lubricants for eyes, joints, and medical implants, as well as in drug delivery systems. Braunschweig said more uses for snail mucus are being discovered every day.

Shi Chen, CUNY ASRC researcher and professor at CUNY Graduate Center and Mandy Holford, professor of chemistry at CUNY Graduate Center and Hunter College, were collaborators on the study.

more information:
Antonio R. Cirullo et al., Comparative mucosal analysis of three functionally distinct Corno apersum secretions, Nature Communications (2023). doi: 10.1038/s41467-023-41094-z

Journal information:
Nature Communications

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