Interactions between fibroin and sericin proteins from Antheraea pernyi and Bombyx mori silk fibers

Shan Du, Jin Zhang, Wei T. Zhou, Quan X. Li, George W. Greene, Hai J. Zhu, Jing L. Li*, Xun G. Wang

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Silkworm silk fibers are core-shell composites of fibroin and sericin proteins. Studying the interactions between fibroin and sericin is essential for understanding the properties of these composites. It is observed that compared to the domestic silk cocoon Bombyx mori (B. mori), the adhesion between fibroin and sericin from the wild silk cocoon, Antheraea pernyi (A. pernyi), is significantly stronger with a higher degree of heterogeneity. The adsorption of A. pernyi sericin on its fibroin is almost twice the value for B. mori sericin on fibroin, both showing a monolayer Langmuir adsorption. 1H NMR and FTIR studies demonstrate on a molecular level the stronger interactions and the more intensive complex formation between A. pernyi fibroin and sericin, facilitated by the hydrogen bonding between glycine and serine. The findings of this study may help the design of composites with superior interfacial adhesion between different components.

Original languageEnglish
Pages (from-to)316-323
Number of pages8
JournalJournal of Colloid and Interface Science
StatePublished - 15 Sep 2016
Externally publishedYes


  • Fibroin
  • Interfacial adhesion
  • Sericin
  • Silk
  • Surface energy


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