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With advancements in computational molecular modeling and powerful structure search methods, it is now possible to systematically screen crystal structures for small organic molecules. 

Biological systems, including proteins, employ water-mediated supramolecular interactions to adopt specific conformations for their functions. However, current solid-state supramolecular materials are typically stiff and fail to capture the dynamic behaviors observed in proteins. Here, we present dynamic crystal-hydrates of aliphatic dipeptides with sequence-isomers of leucine (L) and isoleucine (I). These crystals exhibit shallow conformational energy landscapes, with various reconfigurable crystal nano-architectures accessible through small changes in relative humidity and temperature. Specifically, for LI crystals, as water content changes, the solid-state supramolecular architecture rapidly and reversibly transitions between perpendicular and parallel honeycomb nano-architectures, as well as layered van der Waals structures, leading to significant and distinct variations in mechanical and photophysical properties. Our findings demonstrate the potential of leveraging aliphatic hydrophobic domains inspired by protein architectures to create dynamic solid-state materials with context-adaptive properties.