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

TY - JOUR

T1 - Interactions between fibroin and sericin proteins from Antheraea pernyi and Bombyx mori silk fibers

AU - Du, Shan

AU - Zhang, Jin

AU - Zhou, Wei T.

AU - Li, Quan X.

AU - Greene, George W.

AU - Zhu, Hai J.

AU - Li, Jing L.

AU - Wang, Xun G.

N1 - Publisher Copyright: © 2016 Elsevier Inc.

PY - 2016/9/15

Y1 - 2016/9/15

N2 - 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.

AB - 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.

KW - Fibroin

KW - Interfacial adhesion

KW - Sericin

KW - Silk

KW - Surface energy

UR - http://www.scopus.com/inward/record.url?scp=84973889781&partnerID=8YFLogxK

U2 - 10.1016/j.jcis.2016.06.030

DO - 10.1016/j.jcis.2016.06.030

M3 - 文章

C2 - 27314644

AN - SCOPUS:84973889781

SN - 0021-9797

VL - 478

SP - 316

EP - 323

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

ER -