<p>Hydrogels, which are three-dimensional crosslinked hydrophilic polymer networks capable of retaining over 90% water content, have garnered significant attention in flexible sensor technologies due to their unique combination of intrinsic flexibility, biocompatibility, and tissue-adhesive properties This study proposed a strategy to tailor the mechanical properties and electrical conductivity of protein hydrogels by immersing them in ammonium sulfate solutions, thereby modulating protein chain aggregation via the Hofmeister effect. The characteristics of the hydrogel, including their chemical structure, microstructure, thermal stability, swelling performance, mechanical properties and conductivity and strain-sensitivity performance, were investigated to assess the effects of ammonium sulfate on the egg white hydrogel and evaluate the potential application in the field of wearable sensing technology. Results demonstrate that ammonium sulfate affected hydrogen bonding and the secondary structure of protein chains, leading to protein aggregation and a denser three-dimensional network microstructure. The Hofmeister effect endowed the hydrogels with exceptional thermal stability, excellent freezing resistance (&lt; − 20&#xa0;°C), and remarkable swelling resistance. The compressive fracture strength of the ammonium sulfate-immersed hydrogels were improved to 5.0 times and 8.8 times that of the original egg white protein hydrogels, respectively. Also, the electrical conductivity reached 4.93 S/m. The ammonium sulfate-immersed hydrogels exhibited stable and sensitive electrical signal transmission performance, which could accurately monitor the movement of many joints in the human body as strain sensors. Thus, we developed a facile single-step salt-assisted immersion strategy to fabricate mechanically robust, naturally derived protein-based hydrogels with great potential for motion detection and information recording.</p> Graphical abstract <p></p>

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A tough and conductive egg white protein hydrogel constructed based on the Hofmeister effect for strain sensors

  • Bingchao Duan,
  • Hongdan Hao,
  • Guanyu Zhu,
  • Yufei Wang,
  • Lan Wang,
  • Yuling Li,
  • Lingli Zhang,
  • Congjun Liu,
  • Feifei Meng,
  • Hongyan Yang,
  • Minghui Yang,
  • Xinyue Han,
  • Jiaxin Ma,
  • Ting Wang

摘要

Hydrogels, which are three-dimensional crosslinked hydrophilic polymer networks capable of retaining over 90% water content, have garnered significant attention in flexible sensor technologies due to their unique combination of intrinsic flexibility, biocompatibility, and tissue-adhesive properties This study proposed a strategy to tailor the mechanical properties and electrical conductivity of protein hydrogels by immersing them in ammonium sulfate solutions, thereby modulating protein chain aggregation via the Hofmeister effect. The characteristics of the hydrogel, including their chemical structure, microstructure, thermal stability, swelling performance, mechanical properties and conductivity and strain-sensitivity performance, were investigated to assess the effects of ammonium sulfate on the egg white hydrogel and evaluate the potential application in the field of wearable sensing technology. Results demonstrate that ammonium sulfate affected hydrogen bonding and the secondary structure of protein chains, leading to protein aggregation and a denser three-dimensional network microstructure. The Hofmeister effect endowed the hydrogels with exceptional thermal stability, excellent freezing resistance (< − 20 °C), and remarkable swelling resistance. The compressive fracture strength of the ammonium sulfate-immersed hydrogels were improved to 5.0 times and 8.8 times that of the original egg white protein hydrogels, respectively. Also, the electrical conductivity reached 4.93 S/m. The ammonium sulfate-immersed hydrogels exhibited stable and sensitive electrical signal transmission performance, which could accurately monitor the movement of many joints in the human body as strain sensors. Thus, we developed a facile single-step salt-assisted immersion strategy to fabricate mechanically robust, naturally derived protein-based hydrogels with great potential for motion detection and information recording.

Graphical abstract