Authors
Tai-De Li, Advanced Science Research Center (ASRC) at the Graduate Center, City University of New York
Rein Ulijn, Advanced Science Research Center (ASRC) at the Graduate Center, City University of New York
Short peptides are commonly used to construct supramolecular materials. Most reported peptide materials are hydrophobic and stiff and show a limited response to external stimuli in the solid state. In this work, we describe a series of supramolecular metallo-peptide nanofibers that, depending on their sequence, change stiffness and reversibly assemble in the solid state in response to changes in relative humidity (RH). We tested a histidine (H) series containing dipeptides with varying hydrophobicities, XH, where X is Glycine(G), Alanine(A), Leucine(L), and tyrosine(Y). Metal coordination with Zinc and dynamic H-bonds supports the one-dimensional fiber formation. Specifically, the solvent mixture was tuned for GH/Zn and AH/Zn sequences to obtain gels that gave rise to nanofibers upon air-drying. When these nanofiber networks were exposed to high relative humidity, a reduction in stiffness and a reversible disassembly between 60–70 % RH were observed. This assembly/disassembly process was possible because of the balance of hydrogen bonding interactions between the peptides and water. The RH-responsive actuation was tested upon the deposition of these nanofibers on the surface of a polyimide film; when the relative humidity varied, the peptide/water interactions in the solid state mechanically transferred to the polymer film, resulting in the rapid and reversible folding-unfolding of the films. Thus, demonstrating the possibility of using this material as a mechanical actuator.