Foldamer–protein pair unlocks precise building blocks for artificial molecular materials

Aug, Wed, 2026
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Proteins form complex three-dimensional shapes and can join together to create larger structures. Researchers want to use these properties to make artificial materials. However, arranging proteins and synthetic molecules together with a high level of structural precision is no easy task. This is partly because of the lack of large, clearly defined contact surfaces between the two components.

Light-driven proteins in artificial membranes—a new method for biohybrid systems
Light-driven membrane proteins are key components in biohybrid systems because they can convert light energy into ion gradients, enabling energy conversion or sensory applications. While their integration into natural lipid membranes is well studied, embedding them in artificial polymer membranes has proven challenging.
Foldamer–protein pair unlocks precise building blocks for artificial molecular materials
Proteins form complex three-dimensional shapes and can join together to create larger structures. Researchers want to use these properties to make artificial materials. However, arranging proteins and synthetic molecules together with a high level of structural precision is no easy task. This is partly because of the lack of large, clearly defined contact surfaces between the two components.
Reusing liquid pickle waste to produce omega-3 fatty acids
Docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA) are omega-3 fatty acids known to have beneficial effects and are popular as functional foods and dietary supplements. They are polyunsaturated fatty acids (PUFAs); the primary source of these PUFAs for humans is fish oil.
Deep-learning approach rapidly predicts where metals bind within proteins
In the living world, roughly a third of all proteins we know rely on metals to function. Zinc helps enzymes break down molecules, iron helps carry oxygen in the blood, calcium helps relay signals in cells and potassium flows through channels that help keep our hearts beating. But despite the important role they play, scientists have long struggled to pinpoint exactly where metal ions bind in a protein to get the job done.
Moving nitrogen within pyridine opens a new path for molecular editing
A research team has developed a new molecular editing strategy that can directly convert pyridine compounds into their positional isomers. Instead of moving individual substituents around the molecule, the method relocates the nitrogen atom within the pyridine ring itself, allowing existing molecular structures to be reorganized while preserving their substituents.