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Abstract Polymer brushes have found extensive applications as nano‐scale surface coatings with responsive properties, particularly in achieving tunable friction in solvent environments. Here, a special property of hygroscopic polyelectrolyte‐grafted brushes, where the friction forces change by over two orders of magnitude within a narrow range in humidity is reported. Using mechanical measurements of nano‐scale modulus and water absorption coupled with friction and surface‐sensitive spectroscopy, this sharp change in friction is controlled by a humidity‐induced glass transition that abruptly shifts the mode of sliding is demonstrated. Contrary to expectations based on conventional thinking regarding brush lubrication, friction remains large and humidity‐independent below the glass transition even for systems that absorb as much as 30–40% water by volume. This results in an abrupt change in friction past the glass transition humidity. Tuning the chemistry of brushes and their humidity‐induced glass transition offers the tunability to control the on/off friction (or slipperiness) for nanoactuators, ratchets, and catheters, without the need for externally applied lubricating liquids. 

The spider major ampullate (MA) silk exhibits high tensile strength and extensibility and is typically a blend of MaSp1 and MaSp2 proteins with the latter comprising glycine–proline–glycine–glycine-X repeating motifs that promote extensibility and supercontraction. The MA silk from Darwin's bark spider ( Caerostris darwini ) is estimated to be two to three times tougher than the MA silk from other spider species. Previous research suggests that a unique MaSp4 protein incorporates proline into a novel glycine–proline–glycine–proline motif and may explain C. darwini MA silk's extraordinary toughness. However, no direct correlation has been made between the silk's molecular structure and its mechanical properties for C. darwini . Here, we correlate the relative protein secondary structure composition of MA silk from C. darwini and four other spider species with mechanical properties before and after supercontraction to understand the effect of the additional MaSp4 protein. Our results demonstrate that C. darwini MA silk possesses a unique protein composition with a lower ratio of helices (31%) and β-sheets (20%) than other species. Before supercontraction, toughness, modulus and tensile strength correlate with percentages of β-sheets, unordered or random coiled regions and β-turns. However, after supercontraction, only modulus and strain at break correlate with percentages of β-sheets and β-turns. Our study highlights that additional information including crystal size and crystal and chain orientation is necessary to build a complete structure–property correlation model.