Silk structure and degradation

Colloids Surf B Biointerfaces. 2015 Jul 1:131:122-8. doi: 10.1016/j.colsurfb.2015.04.040. Epub 2015 Apr 24.

Abstract

To investigate the structure of silk and its degradation properties, we have monitored the structure of silk using scanning electron microscopy and frozen sections. Raw silk and degummed raw silk were immersed in four types of degradation solutions for 156 d to observe their degradation properties. The subcutaneous implants in rats were removed after 7, 14, 56, 84, 129, and 145 d for frozen sectioning and subsequent staining with hematoxylin and eosin (H.E.), DAPI, Beta-actin and Collagen I immunofluorescence staining. The in vitro weight loss ratio of raw silk and degummed raw silk in water, PBS, DMEM and DMEM containing 10% FBS (F-DMEM) were, respectively, 14%/11%, 12.5%/12.9%, 11.1%/14.3%, 8.8%/11.6%. Silk began to degrade after 7 d subcutaneous implantation and after 145 d non-degraded silk was still observed. These findings suggest the immunogenicity of fibroin and sericin had no essential difference. In the process of in vitro degradation of silk, the role of the enzyme is not significant. The in vivo degradation of silk is related to phagocytotic activity and fibroblasts may be involved in this process to secrete collagen. This study also shows the developing process of cocoons and raw silk.

Keywords: Bombyx mori L.; Degradation; Fibroin; Silk; Structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bombyx / metabolism*
  • Female
  • Fibroins / metabolism*
  • Insect Proteins / metabolism*
  • Male
  • Microscopy, Confocal
  • Microscopy, Electron, Scanning
  • Prostheses and Implants
  • Proteolysis
  • Rats, Sprague-Dawley
  • Sericins / metabolism*
  • Silk / chemistry
  • Silk / metabolism*
  • Silk / ultrastructure
  • Subcutaneous Tissue / metabolism
  • Subcutaneous Tissue / surgery
  • Time Factors

Substances

  • Insect Proteins
  • Sericins
  • Silk
  • Fibroins