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Under Pressure: Manipulating Protein-mimicking Molecules with Hydrostatic Pressure

Under pressure: Manipulating protein-mimicking molecules with hydrostatic pressure

 E-Mail IMAGE: In the ground state, the host adopts two conformers, one extended and one folded, and gradually shifts to an extended-rich state upon pressurization. Then, in the excited state (hυ), these. view more  Credit: Chemical Science Stimulus-responsive supramolecular structures have emerged as an alternative to conventional ones, owing to their applications in sensing, drug delivery, and switchable memory systems. Now, scientists at Tokyo Institute of Technology explore the hydrostatic-pressure response of foldamers artificial molecules that mimic protein folding and report a shift in their preferred conformation with changing pressure, demonstrating hydrostatic pressure-enabled dynamic control. The finding opens doors to future development of pressure-sensitive foldamers and artificial materials.

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