ArticleLangmuir : the ACS journal of surfaces and colloids2023
Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method.
Article in Langmuir : the ACS journal of surfaces and colloids, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 11 citations in OpenAlex.
- Biosynthetic optical waveguide interface integration using biomimetic -Computational and structural biotechnology journal · 2026Article
- Pollen-inspired biopolymer-based multifunctional films.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Factors Influencing Properties of Spider Silk Coatings and Their Interactions within a Biological Environment.Journal of functional biomaterials · 2023Review
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Authors and funding
5 authors at 2 institutions in 1 country.
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Abstract
Molecular engineering of protein structures offers a uniquely versatile route for novel functionalities in materials. Here, we describe a method to form highly hydrophobic thin films using genetically engineered spider silk proteins. We used structurally engineered protein variants containing ADF3 and AQ12 spider silk sequences. Wetting properties were studied using static and dynamic contact angle measurements. Solution conditions and the surrounding humidity during film preparation were key parameters to obtain high hydrophobicity, as shown by contact angles in excess of 120°. Although the surface layer was highly hydrophobic, its structure was disrupted by the added water droplets. Crystal-like structures were found at the spots where water droplets had been placed. To understand the mechanism of film formation, different variants of the proteins, the topography of the films, and secondary structures of the protein components were studied. The high contact angle in the films demonstrates that the conformations that silk proteins take in the protein layer very efficiently expose their hydrophobic segments. This work reveals a highly amphiphilic nature of silk proteins and contributes to an understanding of their assembly mechanisms. It will also help in designing diverse technical uses for recombinant silk.
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