• Chen, Xi
• Saha, Ranajit
• Dey, Avishek
• Li, Tai-De
• Ulijn, Rein V.
• Zhang, Sheng
• Nair, Maya Narayanan

Abstract

<jats:p>Short peptides are versatile molecules for the construction of supramolecular materials. Most reported peptide materials are hydrophobic, stiff, and show limited response to environmental conditions in the solid‐state. Herein, we describe a design strategy for minimalistic supramolecular metallo‐peptide nanofibers that, depending on their sequence, change stiffness, or reversibly assemble in the solid‐state, in response to changes in relative humidity (RH). We tested a series of histidine (H) containing dipeptides with varying hydrophobicity, XH, where X is G, A, L, Y (glycine, alanine, leucine, and tyrosine). The one‐dimensional fiber formation is supported by metal coordination and dynamic H‐bonds. Solvent conditions were identified where GH/Zn and AH/Zn formed gels that upon air‐drying gave rise to nanofibers. Upon exposure of the nanofiber networks to increasing RH, a reduction in stiffness was observed with GH/Zn fibers reversibly (dis‐)assembled at 60‐70% RH driven by a rebalancing of H‐bonding interactions between peptides and water. When these metallo‐peptide nanofibers were deposited on the surface of polyimide films and exposed to varying RH, peptide/water‐vapor interactions in the solid‐state mechanically transferred to the polymer film, leading to the rapid and reversible folding‐unfolding of the films, thus demonstrating RH‐responsive actuation.</jats:p>

Topics

• impedance spectroscopy
• surface
• polymer
• drying