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

Version 2 2024-06-06, 00:28
Version 1 2016-06-15, 10:24
journal contribution
posted on 2024-06-06, 00:28 authored by S Du, J Zhang, WT Zhou, Sulley LiSulley Li, GW Greene, HJ Zhu, Jingliang LiJingliang Li, XG Wang
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.

History

Journal

Journal of Colloid and Interface Science

Volume

478

Pagination

316-323

Location

United States

ISSN

0021-9797

eISSN

1095-7103

Language

English

Publication classification

C Journal article, C1 Refereed article in a scholarly journal

Copyright notice

2016, Elsevier

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE