Interactions between fibroin and sericin proteins from Antheraea pernyi and Bombyx mori silk fibers.
J Colloid Interface Sci
; 478: 316-23, 2016 Sep 15.
Article
en En
| MEDLINE
| ID: mdl-27314644
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. (1)H 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Bombyx
/
Seda
/
Sericinas
/
Fibroínas
/
Mariposas Nocturnas
Límite:
Animals
Idioma:
En
Revista:
J Colloid Interface Sci
Año:
2016
Tipo del documento:
Article
País de afiliación:
Australia