4.8 Article

Molecular Design and Preparation of Protein-Based Soft Ionic Conductors with Tunable Properties

期刊

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acsami.2c09576

关键词

silk protein; soft ionic conductors; structure-properties relationships; protein-ion interaction; ionic conduction mechanism

资金

  1. foundation of Westlake
  2. National Natural Science Foundation of China [52103129]
  3. foundation of Westlake Multidisciplinary Research Initiative Center [MRIC20210203]
  4. Zhejiang Province Postdoctoral Research Projects
  5. XSEDE program [TG-BIO210063]
  6. U.S. National Science Founda-tion [2038057]
  7. Cornell Universitys faculty startup grant
  8. Instrumentation and Service Centre for Molecular Sciences and Instrumentation and Service Centre for Physical Sciences, Westlake University
  9. Directorate For Engineering
  10. Div Of Civil, Mechanical, & Manufact Inn [2038057] Funding Source: National Science Foundation

向作者/读者索取更多资源

Protein-based soft ionic conductors have great potential in applications at the human-machine interfaces. A new method to fabricate silk-based soft ionic conductors using silk proteins and calcium chloride has been developed. The mechanism of ion transport and molecular interactions between calcium ions and silk proteins at different water contents has been investigated. The results show that the ionic conductivity increases as the distance between calcium ions and silk proteins increases with the increase of water content.
Protein-based soft ionic conductors have attracted considerable research interest in recent years with great potential in applications at the human- machine interfaces. However, a fundamental mechanistic understanding of the ionic conductivity of silk-based ionic conductors is still unclear. Here, we first developed an environmental-friendly and scalable method to fabricate silk-based soft ionic conductors using silk proteins and calcium chloride. The mechanistic understanding of the ion transport and molecular interactions between calcium ions and silk proteins at variable water contents was investigated in-depth by combining experimental and simulation approaches. The results show that calcium ions primarily interact with amide groups in proteins at a low water content. The ionic conductivity is low since the calcium ions are confined around silk proteins within 2.0-2.6 angstrom. As water content increases, the calcium ions are hydrated with the formation of water shells, leading to the increased distance between calcium ions and silk proteins (3.3-6.0 angstrom). As a result, the motion of the calcium ions increased to achieve a higher ionic conductivity. By optimizing the ratio of the silk proteins, calcium ions, and water, silk-based soft ionic conductors with good stretchability and self-healing properties can be obtained. Such protein-based soft ionic conductors can be further used to fabricate smart devices such as electrochromic devices.

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