Abstract

The rapid manufacture of silk fibroin gels in mild conditions is an important subject in the field of silk-based biomaterials. In this study, the gelation of Antheraea pernyi silk fibroin (ASF) aqueous solution was induced by shearing, without chemical cross-linking agents. Simple shearing controlled and accomplished the steady and rapid conformational transition to β-sheets with ease. The conformational transformation and rapid gelation mechanisms of ASF induced by shearing were tracked and analyzed by circular dichroism spectrometry, Fourier transform infrared spectroscopy and X-ray diffractometry, then compared with Bombyx mori silk fibroin (BSF). ASF quickly formed hydrogels within 24 - 48 h after shearing under different shearing rates for 30 - 90 min, resulting in sol-gel transformation when the β-sheet content reached nearly 50%, which is the minimum content needed to maintain a stable hydrogel system in ASF. The gel structures remained stable once formed. The rapid gelation of ASF through shearing compared with BSF was achieved because of ASF’s alternating polyalanine-containing units, which tend to form α-helix structures spontaneously. Further, the entropic cost during the conformational transition from the α-helix to the β-sheet structure is less than the cost of the transition from the random coil structure. This method is a simple, non-chemical cross-linking approach for the promotion of rapid gelation and the protection of the biological properties of ASF, and it may prove useful for application in the field of biomedical materials.

Highlights

  • Silk fibroin (SF) is a natural structural protein excreted from domestic (Bombyx mori) or wild silkworms

  • The conformational transformation and rapid gelation mechanisms of Antheraea pernyi silk fibroin (ASF) induced by shearing were tracked and analyzed by circular dichroism spectrometry, Fourier transform infrared spectroscopy and X-ray diffractometry, compared with Bombyx mori silk fibroin (BSF)

  • The results show that the gelation rate of ASF was significantly faster than the gelation rate of BSF under the same conditions

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Summary

Introduction

Silk fibroin (SF) is a natural structural protein excreted from domestic (Bombyx mori) or wild silkworms The former has been widely used in the textile industry for thousands of years due to its outstanding mechanical properties [1]. As one of the most common species of wild silkworms, Antheraea pernyi silk fibroin (ASF) is characterized by more Ala, Arg and His and fewer Gly amino acid residues than BSF. It contains the tripeptide sequence Arg-GlyAsp (RGD), which is known to be the receptor of cell integrins and to mediate special interactions between mammalian cells [11,12]. The results showed that A. mylitta silk fibroin was superior to BSF due to its RGD

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